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Conserved domains on  [gi|1226745742|ref|WP_093983521|]
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membrane-bound lytic murein transglycosylase MltF [Shewanella algae]

Protein Classification

membrane-bound lytic murein transglycosylase F( domain architecture ID 11484996)

membrane-bound lytic murein transglycosylase F (MltF) cleaves the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin to allow for the regular growth and maintenance of the murein sacculus

CATH:  3.40.190.10
EC:  4.2.2.-
Gene Ontology:  GO:0000270|GO:0016837|GO:0008933|GO:0016829|GO:0016020
PubMed:  17468031|18234673

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
1-468 0e+00

membrane-bound lytic murein transglycosylase MltF;


:

Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 735.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742   1 MKRFTATLTLIILLA---------GCRQPVVDEAQVTpAVNEAKELRVGTLYGPQIYVSSTQGSAGFDYEMAARFADFLG 71
Cdd:PRK10859    1 MKRLKINYLFIGLLAlllaaalwpSIPWFSKEENQLE-QIQERGELRVGTINSPLTYYIGNDGPTGFEYELAKRFADYLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  72 KPLEMKPYGNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSS 150
Cdd:PRK10859   80 VKLEIKVRDNISQLFDALDKGKADLAAAGLTYTPERLKQFRFGPPYYSVSQQLVYRKGQPRPRSLGDLkGGTLTVAAGSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 151 FVETLNRLKADNPNLEWQQVADKDNEELLSMIASGELSYTISDSTSININRRFMPELRSGQVLEQQQAVVWLLPPRGSDQ 230
Cdd:PRK10859  160 HVETLQELKKKYPELSWEESDDKDSEELLEQVAEGKIDYTIADSVEISLNQRYHPELAVAFDLTDEQPVAWALPPSGDDS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 231 LMSQLLRFWHQEQRDGTLEHLVEKYFGHVKRFDYVDTRAFIRAVDSKLPKYRHLFETYAGELDWRKLAATSYQESHWNPR 310
Cdd:PRK10859  240 LYAALLDFFNQIKEDGTLARLEEKYFGHVDRFDYVDTRTFLRAIDNRLPKYQPLFEKYAGELDWRLLAAIAYQESHWNPQ 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 311 ARSPTGVRGMMMLTLATAKQLGVENRLDPEQSIRGGARYLSDILVRLPESIPEEERMWFALASYNIGYGHVEDARKLAQA 390
Cdd:PRK10859  320 ATSPTGVRGLMMLTRNTAQSMGVTDRLDPEQSIRGGARYLQDLMERLPESIPEPERIWFALAAYNIGYGHMLDARRLTKK 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 391 RGLNPSAWKDLKQVLPLLQKRKYYQHTRYGYARGNEAVHYVDSIRRYYDTLVWIDNQ--AKLEALAREQAQEEAAQREAE 468
Cdd:PRK10859  400 QGGNPDSWADVKKRLPLLSQKKYYSKTRYGYARGHEAVHYVENIRRYYDSLVGYLQEkeKQAAEEAPQLAQDYPAVSPAE 479
 
Name Accession Description Interval E-value
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
1-468 0e+00

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 735.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742   1 MKRFTATLTLIILLA---------GCRQPVVDEAQVTpAVNEAKELRVGTLYGPQIYVSSTQGSAGFDYEMAARFADFLG 71
Cdd:PRK10859    1 MKRLKINYLFIGLLAlllaaalwpSIPWFSKEENQLE-QIQERGELRVGTINSPLTYYIGNDGPTGFEYELAKRFADYLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  72 KPLEMKPYGNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSS 150
Cdd:PRK10859   80 VKLEIKVRDNISQLFDALDKGKADLAAAGLTYTPERLKQFRFGPPYYSVSQQLVYRKGQPRPRSLGDLkGGTLTVAAGSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 151 FVETLNRLKADNPNLEWQQVADKDNEELLSMIASGELSYTISDSTSININRRFMPELRSGQVLEQQQAVVWLLPPRGSDQ 230
Cdd:PRK10859  160 HVETLQELKKKYPELSWEESDDKDSEELLEQVAEGKIDYTIADSVEISLNQRYHPELAVAFDLTDEQPVAWALPPSGDDS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 231 LMSQLLRFWHQEQRDGTLEHLVEKYFGHVKRFDYVDTRAFIRAVDSKLPKYRHLFETYAGELDWRKLAATSYQESHWNPR 310
Cdd:PRK10859  240 LYAALLDFFNQIKEDGTLARLEEKYFGHVDRFDYVDTRTFLRAIDNRLPKYQPLFEKYAGELDWRLLAAIAYQESHWNPQ 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 311 ARSPTGVRGMMMLTLATAKQLGVENRLDPEQSIRGGARYLSDILVRLPESIPEEERMWFALASYNIGYGHVEDARKLAQA 390
Cdd:PRK10859  320 ATSPTGVRGLMMLTRNTAQSMGVTDRLDPEQSIRGGARYLQDLMERLPESIPEPERIWFALAAYNIGYGHMLDARRLTKK 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 391 RGLNPSAWKDLKQVLPLLQKRKYYQHTRYGYARGNEAVHYVDSIRRYYDTLVWIDNQ--AKLEALAREQAQEEAAQREAE 468
Cdd:PRK10859  400 QGGNPDSWADVKKRLPLLSQKKYYSKTRYGYARGHEAVHYVENIRRYYDSLVGYLQEkeKQAAEEAPQLAQDYPAVSPAE 479
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 10-444 4.58e-174

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 495.35  E-value: 4.58e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  10 LIILLAGCRQPVVDeaqvTPAVNEAKELRVGTLYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGNINELYQAL 89
Cdd:COG4623     1 LLLLLPACSSEPGD----LEQIKERGVLRVLTRNSPTTYFIYRGGPMGFEYELAKAFADYLGVKLEIIVPDNLDELLPAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  90 KQNEIDLIAAGLSDTRSRRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSSFVETLNRLKADNPNLEWQ 168
Cdd:COG4623    77 NAGEGDIAAAGLTITPERKKQVRFSPPYYSVSQVLVYRKGSPRPKSLEDLaGKTVHVRAGSSYAERLKQLNQEGPPLKWE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 169 QVADKDNEELLSMIASGELSYTISDSTSININRRFMPELRSGQVLEQQQAVVWLLPpRGSDQLMSQLLRFWHQEQRDGTL 248
Cdd:COG4623   157 EDEDLETEDLLEMVAAGEIDYTVADSNIAALNQRYYPNLRVAFDLSEPQPIAWAVR-KNDPSLLAALNEFFAKIKKGGTL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 249 EHLVEKYFGHVKRfdyvDTRAFIRAVDSKLPKYRHLFETYAGE--LDWRKLAATSYQESHWNPRARSPTGVRGMMMLTLA 326
Cdd:COG4623   236 ARLYERYFGHVKR----DTRAFLRRIEGRLPPYDPLFEKYAEEygLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 327 TAKQLGVENRLDPEQSIRGGARYLSDILVRLPESIPEEERMWFALASYNIGYGHVEDARKLAQARGLNPSAWKDLKQvlp 406
Cdd:COG4623   312 TAKELGVDDRLDPEQSIRAGAKYLRWLYDRFPEAIDEPDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFDVEK--- 388

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1226745742 407 llQKRKYYQHtryGYARGNEAVHYVDSIRRYYDTLVWI 444
Cdd:COG4623   389 --SQPKYYDT---GYARGRETVNYVPNIRAYYDIYKRL 421
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 285-443 2.93e-86

membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381606 [Multi-domain]  Cd Length: 161  Bit Score: 261.70  E-value: 2.93e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 285 FETYAGE--LDWRKLAATSYQESHWNPRARSPTGVRGMMMLTLATAKQLGVENRLDPEQSIRGGARYLSDILVRLPESIP 362
Cdd:cd13403     1 FKKYAEKygFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGVNDRLDPEQNIHAGAKYLRYLRDRFPPDID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 363 EEERMWFALASYNIGYGHVEDARKLAQARGLNPSAWKDLKQVLPLLQKRKYYQHTRYGYARGNEAVHYVDSIRRYYDTLV 442
Cdd:cd13403    81 EPDRLKFALAAYNAGPGHVRDARRLAKKYGLNPNVWFDNVEVLPLLKSPYYDPVVKYGYARGRETVNYVRNIRKYYDAYK 160


                  .
gi 1226745742 443 W 443
Cdd:cd13403   161 Q 161
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
 37-256 5.80e-31

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 119.32  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  37 LRVGTL--YGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPyGNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLG 114
Cdd:pfam00497   1 LRVGTDgdYPPFEYVDENGKLVGFDVDLAKAIAKRLGVKVEFVP-VSWDGLIPALQSGKVDLIIAGMTITPERAKQVDFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 115 PPLYRVNQVMVYRAGTPvPKDLNALDA----PVTVIADSSFVETLNRLKADNPNLewqqVADKDNEELLSMIASGELSYT 190
Cdd:pfam00497  80 DPYYYSGQVILVRKKDS-SKSIKSLADlkgkTVGVQKGSTAEELLKNLKLPGAEI----VEYDDDAEALQALANGRVDAV 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1226745742 191 ISDSTSININRRFMPELR---SGQVLEQQQavVWLLPPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYF 256
Cdd:pfam00497 155 VADSPVAAYLIKKNPGLNlvvVGEPLSPEP--YGIAVRKGDPELLAAVNKALAELKADGTLAKIYEKWF 221
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
 36-256 3.55e-30

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 117.04  E-value: 3.55e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742   36 ELRVGTLYG--PQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYgNINELYQALKQNEIDLIAAGLSDTRSRRQQFRL 113
Cdd:smart00062   1 TLRVGTNGDypPFSFADEDGELTGFDVDLAKAIAKELGLKVEFVEV-SFDSLLTALKSGKIDVVAAGMTITPERAKQVDF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  114 GPPLYRVNQVMVYRAGTPvPKDLNALDA-PVTVIADSSFVETLNRLkadNPNLEWQQVadKDNEELLSMIASGELSYTIS 192
Cdd:smart00062  80 SDPYYRSGQVILVRKDSP-IKSLEDLKGkKVAVVAGTTAEELLKKL---YPEAKIVSY--DSNAEALAALKAGRADAAVA 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1226745742  193 DSTSIN--INRRFMPELRSGQVLEQQQAVVWLLPPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYF 256
Cdd:smart00062 154 DAPLLAalVKQHGLPELKIVPDPLDTPEGYAIAVRKGDPELLDKINKALKELKADGTLKKISEKWF 219
 
Name Accession Description Interval E-value
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
1-468 0e+00

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 735.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742   1 MKRFTATLTLIILLA---------GCRQPVVDEAQVTpAVNEAKELRVGTLYGPQIYVSSTQGSAGFDYEMAARFADFLG 71
Cdd:PRK10859    1 MKRLKINYLFIGLLAlllaaalwpSIPWFSKEENQLE-QIQERGELRVGTINSPLTYYIGNDGPTGFEYELAKRFADYLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  72 KPLEMKPYGNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSS 150
Cdd:PRK10859   80 VKLEIKVRDNISQLFDALDKGKADLAAAGLTYTPERLKQFRFGPPYYSVSQQLVYRKGQPRPRSLGDLkGGTLTVAAGSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 151 FVETLNRLKADNPNLEWQQVADKDNEELLSMIASGELSYTISDSTSININRRFMPELRSGQVLEQQQAVVWLLPPRGSDQ 230
Cdd:PRK10859  160 HVETLQELKKKYPELSWEESDDKDSEELLEQVAEGKIDYTIADSVEISLNQRYHPELAVAFDLTDEQPVAWALPPSGDDS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 231 LMSQLLRFWHQEQRDGTLEHLVEKYFGHVKRFDYVDTRAFIRAVDSKLPKYRHLFETYAGELDWRKLAATSYQESHWNPR 310
Cdd:PRK10859  240 LYAALLDFFNQIKEDGTLARLEEKYFGHVDRFDYVDTRTFLRAIDNRLPKYQPLFEKYAGELDWRLLAAIAYQESHWNPQ 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 311 ARSPTGVRGMMMLTLATAKQLGVENRLDPEQSIRGGARYLSDILVRLPESIPEEERMWFALASYNIGYGHVEDARKLAQA 390
Cdd:PRK10859  320 ATSPTGVRGLMMLTRNTAQSMGVTDRLDPEQSIRGGARYLQDLMERLPESIPEPERIWFALAAYNIGYGHMLDARRLTKK 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 391 RGLNPSAWKDLKQVLPLLQKRKYYQHTRYGYARGNEAVHYVDSIRRYYDTLVWIDNQ--AKLEALAREQAQEEAAQREAE 468
Cdd:PRK10859  400 QGGNPDSWADVKKRLPLLSQKKYYSKTRYGYARGHEAVHYVENIRRYYDSLVGYLQEkeKQAAEEAPQLAQDYPAVSPAE 479
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 10-444 4.58e-174

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 495.35  E-value: 4.58e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  10 LIILLAGCRQPVVDeaqvTPAVNEAKELRVGTLYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGNINELYQAL 89
Cdd:COG4623     1 LLLLLPACSSEPGD----LEQIKERGVLRVLTRNSPTTYFIYRGGPMGFEYELAKAFADYLGVKLEIIVPDNLDELLPAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  90 KQNEIDLIAAGLSDTRSRRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSSFVETLNRLKADNPNLEWQ 168
Cdd:COG4623    77 NAGEGDIAAAGLTITPERKKQVRFSPPYYSVSQVLVYRKGSPRPKSLEDLaGKTVHVRAGSSYAERLKQLNQEGPPLKWE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 169 QVADKDNEELLSMIASGELSYTISDSTSININRRFMPELRSGQVLEQQQAVVWLLPpRGSDQLMSQLLRFWHQEQRDGTL 248
Cdd:COG4623   157 EDEDLETEDLLEMVAAGEIDYTVADSNIAALNQRYYPNLRVAFDLSEPQPIAWAVR-KNDPSLLAALNEFFAKIKKGGTL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 249 EHLVEKYFGHVKRfdyvDTRAFIRAVDSKLPKYRHLFETYAGE--LDWRKLAATSYQESHWNPRARSPTGVRGMMMLTLA 326
Cdd:COG4623   236 ARLYERYFGHVKR----DTRAFLRRIEGRLPPYDPLFEKYAEEygLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 327 TAKQLGVENRLDPEQSIRGGARYLSDILVRLPESIPEEERMWFALASYNIGYGHVEDARKLAQARGLNPSAWKDLKQvlp 406
Cdd:COG4623   312 TAKELGVDDRLDPEQSIRAGAKYLRWLYDRFPEAIDEPDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFDVEK--- 388

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1226745742 407 llQKRKYYQHtryGYARGNEAVHYVDSIRRYYDTLVWI 444
Cdd:COG4623   389 --SQPKYYDT---GYARGRETVNYVPNIRAYYDIYKRL 421
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 285-443 2.93e-86

membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381606 [Multi-domain]  Cd Length: 161  Bit Score: 261.70  E-value: 2.93e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 285 FETYAGE--LDWRKLAATSYQESHWNPRARSPTGVRGMMMLTLATAKQLGVENRLDPEQSIRGGARYLSDILVRLPESIP 362
Cdd:cd13403     1 FKKYAEKygFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTARELGVNDRLDPEQNIHAGAKYLRYLRDRFPPDID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 363 EEERMWFALASYNIGYGHVEDARKLAQARGLNPSAWKDLKQVLPLLQKRKYYQHTRYGYARGNEAVHYVDSIRRYYDTLV 442
Cdd:cd13403    81 EPDRLKFALAAYNAGPGHVRDARRLAKKYGLNPNVWFDNVEVLPLLKSPYYDPVVKYGYARGRETVNYVRNIRKYYDAYK 160


                  .
gi 1226745742 443 W 443
Cdd:cd13403   161 Q 161
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
 35-257 4.71e-72

The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270230 [Multi-domain]  Cd Length: 223  Bit Score: 227.48  E-value: 4.71e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  35 KELRVGTLYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLG 114
Cdd:cd01009     1 GELRVLTRNSPTTYYIDRGGPRGFEYELAKAFADYLGVELEIVPADNLEELLEALEEGKGDLAAAGLTITPERKKKVDFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 115 PPLYRVNQVMVYRAGTPVPKDLNALDAP-VTVIADSSFVETLNRLKADNPNLEWQQVADKDNEELLSMIASGELSYTISD 193
Cdd:cd01009    81 FPYYYVVQVLVYRKGSPRPRSLEDLSGKtIAVRKGSSYAETLQKLNKGGPPLTWEEVDEALTEELLEMVAAGEIDYTVAD 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1226745742 194 STSININRRFMPELRSGQVLEQQQAVVWLLPPrGSDQLMSQLLRFWHQEQRDGTLEHLVEKYFG 257
Cdd:cd01009   161 SNIAALWRRYYPELRVAFDLSEPQPLAWAVRK-NSPSLLAALNRFLAQIKKDGTLARLYERYYG 223
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
 37-256 5.80e-31

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 119.32  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  37 LRVGTL--YGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPyGNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLG 114
Cdd:pfam00497   1 LRVGTDgdYPPFEYVDENGKLVGFDVDLAKAIAKRLGVKVEFVP-VSWDGLIPALQSGKVDLIIAGMTITPERAKQVDFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 115 PPLYRVNQVMVYRAGTPvPKDLNALDA----PVTVIADSSFVETLNRLKADNPNLewqqVADKDNEELLSMIASGELSYT 190
Cdd:pfam00497  80 DPYYYSGQVILVRKKDS-SKSIKSLADlkgkTVGVQKGSTAEELLKNLKLPGAEI----VEYDDDAEALQALANGRVDAV 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1226745742 191 ISDSTSININRRFMPELR---SGQVLEQQQavVWLLPPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYF 256
Cdd:pfam00497 155 VADSPVAAYLIKKNPGLNlvvVGEPLSPEP--YGIAVRKGDPELLAAVNKALAELKADGTLAKIYEKWF 221
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
 36-256 3.55e-30

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 117.04  E-value: 3.55e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742   36 ELRVGTLYG--PQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYgNINELYQALKQNEIDLIAAGLSDTRSRRQQFRL 113
Cdd:smart00062   1 TLRVGTNGDypPFSFADEDGELTGFDVDLAKAIAKELGLKVEFVEV-SFDSLLTALKSGKIDVVAAGMTITPERAKQVDF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  114 GPPLYRVNQVMVYRAGTPvPKDLNALDA-PVTVIADSSFVETLNRLkadNPNLEWQQVadKDNEELLSMIASGELSYTIS 192
Cdd:smart00062  80 SDPYYRSGQVILVRKDSP-IKSLEDLKGkKVAVVAGTTAEELLKKL---YPEAKIVSY--DSNAEALAALKAGRADAAVA 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1226745742  193 DSTSIN--INRRFMPELRSGQVLEQQQAVVWLLPPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYF 256
Cdd:smart00062 154 DAPLLAalVKQHGLPELKIVPDPLDTPEGYAIAVRKGDPELLDKINKALKELKADGTLKKISEKWF 219
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
 37-257 2.94e-27

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 108.91  E-value: 2.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  37 LRVGTL--YGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYgNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLG 114
Cdd:COG0834     1 LRVGVDpdYPPFSFRDEDGKLVGFDVDLARAIAKRLGLKVEFVPV-PWDRLIPALQSGKVDLIIAGMTITPEREKQVDFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 115 PPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSSFVEtlnRLKADNPNLEWQQVadKDNEELLSMIASGELSYTISD 193
Cdd:COG0834    80 DPYYTSGQVLLVRKDNSGIKSLADLkGKTVGVQAGTTYEE---YLKKLGPNAEIVEF--DSYAEALQALASGRVDAVVTD 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1226745742 194 STSIN--INRRFMPELR-SGQVLEQQQAVVWLlpPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYFG 257
Cdd:COG0834   155 EPVAAylLAKNPGDDLKiVGEPLSGEPYGIAV--RKGDPELLEAVNKALAALKADGTLDKILEKWFG 219
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 287-392 1.78e-22

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 91.98  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 287 TYAGELDWRKLAATSYQESHWNPRARSPTGVRGMMMLTLATAKQLG------VENRLDPEQSIRGGARYLSDILVRLPES 360
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGlrvnpgVDDLFDPEKNIKAGTKYLKELYKQYGGD 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1226745742 361 IpeeermWFALASYNIGYGHVEDARKLAQARG 392
Cdd:pfam01464  85 L------WLALAAYNAGPGRVRKWIKNAGAKD 110
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
 36-255 2.67e-21

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 91.93  E-value: 2.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  36 ELRVGTL--YGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGnINELYQALKQNEIDLIAAGLSDTRSRRQQFRL 113
Cdd:cd13530     1 TLRVGTDadYPPFEYIDKNGKLVGFDVDLANAIAKRLGVKVEFVDTD-FDGLIPALQSGKIDVAISGMTITPERAKVVDF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 114 GPPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSSFVEtlnRLKADNPNLEWQQVadKDNEELLSMIASGELSYTIS 192
Cdd:cd13530    80 SDPYYYTGQVLVVKKDSKITKTVADLkGKKVGVQAGTTGED---YAKKNLPNAEVVTY--DNYPEALQALKAGRIDAVIT 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1226745742 193 DSTSIN-INRRFMPELRSGQVLEQQQAVVWLLPPrGSDQLMSQLLRFWHQEQRDGTLEHLVEKY 255
Cdd:cd13530   155 DAPVAKyYVKKNGPDLKVVGEPLTPEPYGIAVRK-GNPELLDAINKALAELKADGTLDKLLEKW 217
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 303-386 6.54e-21

lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381594 [Multi-domain]  Cd Length: 111  Bit Score: 87.65  E-value: 6.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 303 QESHWNPRARSPTGVRGMMMLTLATAKQLG---VENRLDPEQSIRGGARYLSDILVRLPESIpeeermWFALASYNIGYG 379
Cdd:cd00254    10 VESGFNPRAVSPAGARGLMQLMPGTARDLGrrgVDDLFDPEENIRAGARYLRELLDRFGGDL------ELALAAYNAGPG 83


                  ....*..
gi 1226745742 380 HVEDARK 386
Cdd:cd00254    84 AVDRWGG 90
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
 35-217 1.10e-19

The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 87.59  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  35 KELRVGTL--YGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGNINELYQALKQNEIDLIAAgLSDTRSRRQQFR 112
Cdd:cd01007     2 PVIRVGVDpdWPPFEFIDEGGEPQGIAADYLKLIAKKLGLKFEYVPGDSWSELLEALKAGEIDLLSS-VSKTPEREKYLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 113 LGPPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSSFVEtlnRLKADNPNLEWQQVadKDNEELLSMIASGELSYTI 191
Cdd:cd01007    81 FTKPYLSSPLVIVTRKDAPFINSLSDLaGKRVAVVKGYALEE---LLRERYPNINLVEV--DSTEEALEAVASGEADAYI 155

                         170       180
                  ....*....|....*....|....*....
gi 1226745742 192 SDSTSIN--INRRFMPELR-SGQVLEQQQ 217
Cdd:cd01007   156 GNLAVASylIQKYGLSNLKiAGLTDYPQD 184
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 213-386 1.38e-17

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 81.97  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 213 LEQQQAVVWLLPPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYFGHVKRFDYVDTRAF-IRAVDSKLP-KYRHLFETYAG 290
Cdd:COG0741    33 AALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLaLAALLLRRPlPYLPLIEEAAK 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 291 E--LDWRKLAATSYQESHWNPRARSPTGVRGMMMLTLATAKQLGV--------ENRLDPEQSIRGGARYLSDILVRLPES 360
Cdd:COG0741   113 KygVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLklglgpspDDLFDPETNIRAGAAYLRELLDRFDGD 192

                         170       180
                  ....*....|....*....|....*.
gi 1226745742 361 IPeeermwFALASYNIGYGHVEDARK 386
Cdd:COG0741   193 LV------LALAAYNAGPGRVRRWLR 212
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 281-398 1.13e-13

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 68.27  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 281 YRHLFETYAGE--LDWRKLAATSYQESHWNPRARSPTGVRGMMMLTLATAK----QLGVENR-----LDPEQSIRGGARY 349
Cdd:cd13401     6 YRDLVERAAKKngLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATAKdvakKLGLPYYsprdlFDPEYNIRLGSAY 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1226745742 350 LSDILVRLPESIPeeermwFALASYNIGYGHVedARKLAQARGLNPSAW 398
Cdd:cd13401    86 LAELLDRFDGNPV------LALAAYNAGPGRV--RRWLKRRGDLDPDLW 126
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
 75-233 2.33e-13

The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270425 [Multi-domain]  Cd Length: 221  Bit Score: 69.17  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  75 EMKPYGNINELYQALKQNEIDLIAAgLSDTRSRRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNALDAPVTVIADSSFVEt 154
Cdd:cd13707    44 EVVRASSPAEMIEALRSGEADMIAA-LTPSPEREDFLLFTRPYLTSPFVLVTRKDAAAPSSLEDLAGKRVAIPAGSALE- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 155 lNRLKADNPNLEWQQVAdkDNEELLSMIASGELSYTISDSTSIN--INRRFMPELRSGQVLEQQQAVVWLLPPRGSDQLM 232
Cdd:cd13707   122 -DLLRRRYPQIELVEVD--NTAEALALVASGKADATVASLISARylINHYFRDRLKIAGILGEPPAPIAFAVRRDQPELL 198


                  .
gi 1226745742 233 S 233
Cdd:cd13707   199 S 199
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 297-402 8.60e-12

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 62.15  E-value: 8.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 297 LAATSYQESHWNPRARSPTGVRGMMMLTLATAKQLGVEN------RLDPEQSIRGGARYLSDILVRLpesipeeeRMWF- 369
Cdd:cd16894    10 LKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVdswvdeRRDPEKSTRAAARYLKDLYKRF--------GDWLl 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1226745742 370 ALASYNIGYGHVedARKLAQARGLNPSAWKDLK 402
Cdd:cd16894    82 ALAAYNAGEGRV--RRAIKRAGTDKWEDYYRLY 112
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
 56-256 3.20e-10

The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 59.91  E-value: 3.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  56 AGFDYEMAARFADFLGKPLEMKPyGNINELYQALKQNEIDLIAaGLSDTRSRRQQFRLGPPLYRVNQVMVYRAGTPVPKD 135
Cdd:cd13704    25 TGFNVDLLRAIAEEMGLKVEIRL-GPWSEVLQALENGEIDVLI-GMAYSEERAKLFDFSDPYLEVSVSIFVRKGSSIINS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 136 LNALDAPVTVIADSSFVETLnrLKADNPNLEWQQVADKdnEELLSMIASGELSYTISDSTSIN--INRRFMPELR-SGQV 212
Cdd:cd13704   103 LEDLKGKKVAVQRGDIMHEY--LKERGLGINLVLVDSP--EEALRLLASGKVDAAVVDRLVGLylIKELGLTNVKiVGPP 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1226745742 213 LEQQQ---AVvwllpPRGSDQLMSQL---LRfwhQEQRDGTLEHLVEKYF 256
Cdd:cd13704   179 LLPLKycfAV-----RKGNPELLAKLnegLA---ILKASGEYDEIYEKWF 220
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 280-439 4.08e-10

uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381617 [Multi-domain]  Cd Length: 146  Bit Score: 57.91  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 280 KYRHLFETYAGE--LDWRKLAATSYQESHWNPRARSPTGVRGMMMLTLATA----KQLGVENR-----LDPEQSIRGGAR 348
Cdd:cd16896     3 KYREYIEKYAKEygVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETAewiaEKLGLEDFseddlYDPETNIRLGTW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 349 YLSDILVRLPESIPeeermwFALASYNIGYGHVEdarklaqaRGLNPSAWKDLKQVLpllqKRKYYQHTRygyargneav 428
Cdd:cd16896    83 YLSYLLKEFDGNLV------LALAAYNAGPGNVD--------KWLKDGGWSGDGKTL----DQIPFPETR---------- 134

                         170
                  ....*....|.
gi 1226745742 429 HYVDSIRRYYD 439
Cdd:cd16896   135 HYVKKVLKNYK 145
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
 36-256 4.26e-10

Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 59.51  E-value: 4.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  36 ELRVGT--LYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYgNINELYQALKQNEIDLIAAGLSDTRSRRQQFRL 113
Cdd:cd13629     1 VLRVGMeaGYPPFEMTDKKGELIGFDVDLAKALAKDLGVKVEFVNT-AWDGLIPALQTGKFDLIISGMTITPERNLKVNF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 114 GPPLYRVNQVMVYR----AGTPVPKDLNALDAPVTVIADSSFVETLNRLkadnpnLEWQQV--ADKDNEELLsMIASGEL 187
Cdd:cd13629    80 SNPYLVSGQTLLVNkksaAGIKSLEDLNKPGVTIAVKLGTTGDQAARKL------FPKATIlvFDDEAAAVL-EVVNGKA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 188 SYTISDSTSI-NINRRFMPELRSGQVLEQQQAVVWLLpPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYF 256
Cdd:cd13629   153 DAFIYDQPTPaRFAKKNDPTLVALLEPFTYEPLGFAI-RKGDPDLLNWLNNFLKQIKGDGTLDELYDKWF 221
PBP2_PheC cd01069
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ...
 33-256 6.23e-10

Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes cyclohexadienyl dehydratase PheC. These proteins catalyze the decarboxylation of prephenate to phenylpyruvate in the alternative phenylalanine biosynthesis pathway in some proteobacteria and archaea. The PheC proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Since they the PheC proteins are so similar to periplasmic binding proteins, (PBP), it is evolutionarily plausible that several pre-existing PBP proteins might have been recruited to perform the enzymatic function.


Pssm-ID: 270231 [Multi-domain]  Cd Length: 232  Bit Score: 59.28  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  33 EAKELRVGTL--YGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKP--YGNineLYQALKQNEIDLIAAGLSDTRSRR 108
Cdd:cd01069     8 ERGVLRVGTTgdYKPFTYRDNQGQYEGYDIDMAEALAKSLGVKVEFVPtsWPT---LMDDLAADKFDIAMGGISITLERQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 109 QQFRLGPPLYRVNQVMVYRAGTpvpKD----LNALDAP-VTVIA-----DSSFVetlnrlkadNPNLEWQQVAD-KDNEE 177
Cdd:cd01069    85 RQAFFSAPYLRFGKTPLVRCAD---VDrfqtLEAINRPgVRVIVnpggtNEKFV---------RANLKQATITVhPDNLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 178 LLSMIASGELSYTISDSTSININRRFMPELrsGQVLEQQQAV----VWLLpPRGSDQLMSQLLRFWHQEQRDGTLEHLVE 253
Cdd:cd01069   153 IFQAIADGKADVMITDAVEARYYQKLDPRL--CAVHPDKPFTfsekAYMI-PRDDQALKRYVDQWLHIMEGSGLLDQLSN 229


                  ...
gi 1226745742 254 KYF 256
Cdd:cd01069   230 KWL 232
PHA00368 PHA00368
internal virion protein D
 294-356 7.74e-10

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 61.72  E-value: 7.74e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1226745742  294 WRKLAatsYQESHWNPRARSPTGVRGMMMLTLATAKQLGV----ENRLDPEQSIRGGARYLSDILVR 356
Cdd:PHA00368    29 LRKVG---WDESRFNPTAKSPTGPKGLMQFTKATAKALGLivddDDRLDPELAIDAGARYLADLVGK 92
PBP2_BvgS_D1 cd13705
The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
 35-208 1.10e-09

The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270423 [Multi-domain]  Cd Length: 221  Bit Score: 58.37  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  35 KELRVGTL---YGPQIYVSST---QG-SAgfDYemAARFADFLGKPLEMKPYGNINELYQALKQNEIDLIAAGLSDtRSR 107
Cdd:cd13705     2 RTLRVGVSapdYPPFDITSSGgryEGiTA--DY--LGLIADALGVRVEVRRYPDREAALEALRNGEIDLLGTANGS-EAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 108 RQQFRLGPPLYRVNQVMVYRAGTPVPKDLNALDAPVTVIADSSFVETlnrLKADNPNLEWQQVAdkDNEELLSMIASGEL 187
Cdd:cd13705    77 DGGLLLSQPYLPDQPVLVTRIGDSRQPPPDLAGKRVAVVPGYLPAEE---IKQAYPDARIVLYP--SPLQALAAVAFGQA 151

                         170       180
                  ....*....|....*....|...
gi 1226745742 188 SYTISDSTSIN--INRRFMPELR 208
Cdd:cd13705   152 DYFLGDAISANylISRNYLNNLR 174
PBP2_AA_binding_like_2 cd13627
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
 31-159 2.03e-09

Substrate-binding domain of putative amino acid-binding protein; the type 2 periplasmic-binding protein fold; This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270345 [Multi-domain]  Cd Length: 243  Bit Score: 57.80  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  31 VNEAKELRVGTLYGPQIYVSstqgsaGFDYEMAARFADFLGKPLEMKPYgNINELYQALKQNEIDLIAAGLSDTRSRRQQ 110
Cdd:cd13627    17 QETASEYAIPIINGQGGYAD------GYDVQIAKKLAEKLDMKLVIKKI-EWNGLIPALNSGDIDLIIAGMSKTPEREKT 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1226745742 111 FRLGPPLYRVNQVMVYRAGTPVPKDLNALD---APVTVIADSSFVETLNRLK 159
Cdd:cd13627    90 IDFSDPYYISNIVMVVKKDSAYANATNLSDfkgATITGQLGTMYDDVIDQIP 141
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
 37-257 5.74e-09

Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein fold; Cystine-binding domain of periplasmic receptor-dependent ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Also, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270344 [Multi-domain]  Cd Length: 219  Bit Score: 56.17  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  37 LRVGT--LYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPyGNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLG 114
Cdd:cd13626     2 LTVGTegTYPPFTFKDEDGKLTGFDVEVGREIAKRLGLKVEFKA-TEWDGLLPGLNSGKFDVIANQVTITPEREEKYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 115 PPLYRVNQVMVYRAGTPVPKDLNALDA-PVTVIADSSFVETLNrlKADNPnleWQQVADKDNEELLSMIASGELSYTISD 193
Cdd:cd13626    81 DPYLVSGAQIIVKKDNTIIKSLEDLKGkVVGVSLGSNYEEVAR--DLANG---AEVKAYGGANDALQDLANGRADATLND 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1226745742 194 ST-SININRRFMPELR-SGQVLEQQQAVVWLlpPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYFG 257
Cdd:cd13626   156 RLaALYALKNSNLPLKiVGDIVSTAKVGFAF--RKDNPELRKKVNKALAEMKADGTLKKLSEKWFG 219
PBP2_ArtJ cd00999
The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold ...
 36-139 1.12e-08

The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold protein superfamily; An arginine-binding protein found in Chlamydiae trachomatis (CT-ArtJ) and pneumoniae (CPn-ArtJ) and its closely related proteins. CT- and CPn-ArtJ are shown to have different immunogenic properties despite a high sequence similarity. The ArtJ proteins display the type 2 periplasmic binding fold organized in two alpha-beta domains with arginine-binding region at their interface.


Pssm-ID: 270220 [Multi-domain]  Cd Length: 223  Bit Score: 55.41  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  36 ELRVGT--LYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGnINELYQALKQNEIDLIAAGLSDTRSRRQQFRL 113
Cdd:cd00999     5 VIIVGTesTYPPFEFRDEKGELVGFDIDLAEAISEKLGKKLEWRDMA-FDALIPNLLTGKIDAIAAGMSATPERAKRVAF 83

                          90       100
                  ....*....|....*....|....*.
gi 1226745742 114 GPPLYRVNQVMVYRAGTPVPKDLNAL 139
Cdd:cd00999    84 SPPYGESVSAFVTVSDNPIKPSLEDL 109
PBP2_polar_AA cd13693
Substrate binding domain of polar amino-acid uptake ABC transporter; the type 2 periplasmic ...
 36-140 3.85e-08

Substrate binding domain of polar amino-acid uptake ABC transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of putative polar amino acid ABC transporter. The polar amino-acid binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270411 [Multi-domain]  Cd Length: 228  Bit Score: 53.86  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  36 ELRVGTL--YGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGNINELyQALKQNEIDLIAAGLSDTRSRRQQFRL 113
Cdd:cd13693     9 KLIVGVKndYPPFGFLDPSGEIVGFEVDLAKDIAKRLGVKLELVPVTPSNRI-QFLQQGKVDLLIATMGDTPERRKVVDF 87

                          90       100
                  ....*....|....*....|....*....
gi 1226745742 114 GPPLYrvnqvmvYRAGTPV--PKDLNALD 140
Cdd:cd13693    88 VEPYY-------YRSGGALlaAKDSGIND 109
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 291-390 8.36e-08

Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381602 [Multi-domain]  Cd Length: 108  Bit Score: 50.38  E-value: 8.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 291 ELDWRKLAATSYQESHWNPRA-RSPTGVRGMMMLTLATAKQLGVE-------NRLDPEQSIRGGARYLSDILVRLpeSIP 362
Cdd:cd13399     2 GVPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMPSTWKAYGVDgngdgkaDPFNPEDAIASAANYLCRHGWDL--NAF 79

                          90       100
                  ....*....|....*....|....*....
gi 1226745742 363 EEERMWFALASYNIG-YGHVEDARKLAQA 390
Cdd:cd13399    80 LGEDNFLALAAYNAGpGAYANAVLELAAT 108
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
 36-139 1.73e-07

Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 periplasmic binding protein fold; This group includes the periplasmic substrate-binding protein ArtJ of the ATP-binding cassette (ABC) transport system from the thermophilic bacterium Geobacillus stearothermophilus, which is specific for arginine, lysine, and histidine. ArtJ belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270342 [Multi-domain]  Cd Length: 219  Bit Score: 51.73  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  36 ELRVGT--LYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGnINELYQALKQNEIDLIAAGLSDTRSRRQQFRL 113
Cdd:cd13624     1 TLVVGTdaTFPPFEFVDENGKIVGFDIDLIKAIAKEAGFEVEFKNMA-FDGLIPALQSGKIDIIISGMTITEERKKSVDF 79

                          90       100
                  ....*....|....*....|....*.
gi 1226745742 114 GPPLYRVNQVMVYRAGTPVPKDLNAL 139
Cdd:cd13624    80 SDPYYEAGQAIVVRKDSTIIKSLDDL 105
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 304-418 4.17e-07

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 49.86  E-value: 4.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 304 ESHWNPRARSPTGVRGMMMLTLATA-----KQLGVENRL-------DPEQSIRGGARYLSdIL-------VRLPESipee 364
Cdd:cd16893    24 ESSFNPYAVSHSPAYGLMQIVPSTAgrdvyRLLGGKGGLpsksylfDPENNIDIGTAYLH-ILqnrylkgIKNPKS---- 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 365 eRMWFALASYNIGYGHV-----EDARK-LAQARGLNPsawkdlKQVLPLLQKRKYYQHTR 418
Cdd:cd16893    99 -REYCAIAAYNGGAGNVlrtfsSDRKKaISKINRLSP------DEVYQHLTKKLPAAETR 151
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
 37-255 6.30e-07

Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 periplasmic binding protein; This periplasmic substrate component serves as an initial receptor in the ABC transport of glutamine in eubacteria and archaea. After binding the alanine with high affinity, this domain Interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. This alanine specific domain belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 50.16  E-value: 6.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  37 LRVGTL--YGP-QIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYgNINELYQALKQNEIDLIAAGLSDTRSRRQQFRL 113
Cdd:cd13628     2 LNMGTSpdYPPfEFKIGDRGKIVGFDIELAKTIAKKLGLKLQIQEY-DFNGLIPALASGQADLALAGITPTPERKKVVDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 114 GPPLYRVNQVMVYRAGTPVPKDLNALDAPVTVIADSSFVETLNRLKADNPNLEWQQVADKDneELLSMIASGELSYTISD 193
Cdd:cd13628    81 SEPYYEASDTIVS*KDRKIKQLQDLNGKSLGVQLGTIQEQLIKELSQPYPGLKTKLYNRVN--ELVQALKSGRVDAAIVE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1226745742 194 STSININRRFMPELRSGQVLEQQQAVVWLLPPRGSdqlmSQLLRF--WHQEQRD-GTLEHLVEKY 255
Cdd:cd13628   159 DIVAETFAQKKN*LLESRYIPKEADGSAIAFPKGS----PLRDDFnrWLKEMGDsGELELMVRRW 219
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 299-382 7.46e-07

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 51.60  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 299 ATSYQESHWNPRARSPTGVRGMMMLTLATA----KQLGVENR------LDPEQSIRGGARYLSDILVRLpesipEEERMw 368
Cdd:PRK11619  499 AIARQESAWNPKARSPVGASGLMQIMPGTAthtvKMFSIPGYssssqlLDPETNINIGTSYLEYVYQQF-----GNNRI- 572

                          90
                  ....*....|....
gi 1226745742 369 FALASYNIGYGHVE 382
Cdd:PRK11619  573 LASAAYNAGPGRVR 586
PBP2_GltS cd13620
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ...
 33-129 1.51e-06

Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 periplasmic binding fold protein superfamily; This family comprises of the periplasmic-binding protein component (GltS) of an ABC transporter specific for glutamate or arginine from Lactococcus lactis, as well as its closely related proteins. The GltS domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis


Pssm-ID: 270338 [Multi-domain]  Cd Length: 227  Bit Score: 49.26  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  33 EAKELRVGTL--YGP---QIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYgNINELYQALKQNEIDLIAAGLSDTRSR 107
Cdd:cd13620     2 KKGKLVVGTSadYAPfefQKMKDGKNQVVGADIDIAKAIAKELGVKLEIKSM-DFDNLLASLQSGKVDMAISGMTPTPER 80

                          90       100
                  ....*....|....*....|..
gi 1226745742 108 RQQFRLGPPLYRVNQVMVYRAG 129
Cdd:cd13620    81 KKSVDFSDVYYEAKQSLLVKKA 102
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 47-147 1.66e-06

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 48.72  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  47 IYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGNINELYQALKQNEIDLIAAGLSDT------RSRRQQFRLGPPLYRV 120
Cdd:cd00648     4 VASIGPPPYAGFAEDAAKQLAKETGIKVELVPGSSIGTLIEALAAGDADVAVGPIAPAleaaadKLAPGGLYIVPELYVG 83

                          90       100
                  ....*....|....*....|....*..
gi 1226745742 121 NQVMVYRAGTPVPKDLNALDAPVTVIA 147
Cdd:cd00648    84 GYVLVVRKGSSIKGLLAVADLDGKRVG 110
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
 36-257 2.10e-06

Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This group contains uncharacterized periplasmic cystine-binding domain of ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270431 [Multi-domain]  Cd Length: 218  Bit Score: 48.43  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  36 ELRVGT--LYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMK--PYGNINElyqALKQNEIDLIAAGLSDTRSRRQQF 111
Cdd:cd13713     1 ELRFAMsgQYPPFNFLDEDNQLVGFDVDVAKAIAKRLGVKVEPVttAWDGIIA---GLWAGRYDIIIGSMTITEERLKVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 112 RLGPPLYRVNQVMVYRAGTPV--PKDLNalDAPVTVIADSSFVETLNRLKadnPNLEWQQVaDKDNEELLSMiASGELSY 189
Cdd:cd13713    78 DFSNPYYYSGAQIFVRKDSTItsLADLK--GKKVGVVTGTTYEAYARKYL---PGAEIKTY-DSDVLALQDL-ALGRLDA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1226745742 190 TISDS-TSININRRFMPELR-SGQVLEQQQAVVWLlpPRGSDQL---MSQLLrfwhQEQR-DGTLEHLVEKYFG 257
Cdd:cd13713   151 VITDRvTGLNAIKEGGLPIKiVGKPLYYEPMAIAI--RKGDPELraaVNKAL----AEMKaDGTLEKISKKWFG 218
PBP2_GluB cd13690
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ...
 33-163 3.15e-06

Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein fold; This group includes periplasmic glutamate-binding domain GluB from Corynebacterium efficiens and its related proteins. The GluB domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270408 [Multi-domain]  Cd Length: 231  Bit Score: 48.42  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  33 EAKELRVGTLYGPQI--YVSSTQGS-AGFDYEMAARFADFLGKP---LEMKPYGNINElYQALKQNEIDLIAAGLSDTRS 106
Cdd:cd13690     6 KRGRLRVGVKFDQPGfsLRNPTTGEfEGFDVDIARAVARAIGGDepkVEFREVTSAER-EALLQNGTVDLVVATYSITPE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1226745742 107 RRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNAL-DAPVTVIADSSfveTLNRLKADNP 163
Cdd:cd13690    85 RRKQVDFAGPYYTAGQRLLVRAGSKIITSPEDLnGKTVCTAAGST---SADNLKKNAP 139
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
 31-137 4.98e-06

Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold; This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270407 [Multi-domain]  Cd Length: 229  Bit Score: 47.61  E-value: 4.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  31 VNEAKELRVGTLYG--PQIYVSSTQGS-AGFDYEMAARFADFLGKPLEMKPYGNINELyQALKQNEIDLIAAGLSDTRSR 107
Cdd:cd13689     4 IKARGVLRCGVFDDvpPFGFIDPKTREiVGFDVDLCKAIAKKLGVKLELKPVNPAARI-PELQNGRVDLVAANLTYTPER 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1226745742 108 RQQFRLGPPLYRVNQVMVYRAGTP--VPKDLN 137
Cdd:cd13689    83 AEQIDFSDPYFVTGQKLLVKKGSGikSLKDLA 114
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
 33-161 7.89e-06

Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate receptor domain GluR0. These domains are found in the GluR0 proteins that have been shown to function as prokaryotic L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. The GluR0 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270218 [Multi-domain]  Cd Length: 218  Bit Score: 46.95  E-value: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  33 EAKELRVGTLYGPQiYVSSTQGS-AGFDYEMAARFADFLGKPLEMKPYGNINELYQALKQNEIDLIAAGLSDTRSRRQQF 111
Cdd:cd00997     1 SAQTLTVATVPRPP-FVFYNDGElTGFSIDLWRAIAERLGWETEYVRVDSVSALLAAVAEGEADIAIAAISITAEREAEF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1226745742 112 RLGPPLYRVN-QVMVyragtPVPKDLNAL-DAP---VTVIADSSFVETLNRLKAD 161
Cdd:cd00997    80 DFSQPIFESGlQILV-----PNTPLINSVnDLYgkrVATVAGSTAADYLRRHDID 129
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
 31-198 1.74e-05

The substrate binding domain of putative amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Agrobacterium tumefaciens and its related proteins. The putative Atu4678-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270414 [Multi-domain]  Cd Length: 227  Bit Score: 45.83  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  31 VNEAKELRVG-TLYGPQIYVSSTQGS-AGFDYEMAARFADFLGKPLEMKPYGNINELyQALKQNEIDLIAAGLSDTRSRR 108
Cdd:cd13696     4 ILSSGKLRCGvCLDFPPFGFRDAAGNpVGYDVDYAKDLAKALGVKPEIVETPSPNRI-PALVSGRVDVVVANTTRTLERA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 109 QQFRLGPPLYRVNQVMVYRAGTPVP--KDLNAldAPVTVIAdSSFVETLnrLKADNPNLEWQQVaDKDNEELLSmIASGE 186
Cdd:cd13696    83 KTVAFSIPYVVAGMVVLTRKDSGIKsfDDLKG--KTVGVVK-GSTNEAA--VRALLPDAKIQEY-DTSADAILA-LKQGQ 155

                         170
                  ....*....|..
gi 1226745742 187 LSYTISDSTSIN 198
Cdd:cd13696   156 ADAMVEDNTVAN 167
PRK15437 PRK15437
histidine ABC transporter substrate-binding protein HisJ; Provisional
 1-256 3.33e-05

histidine ABC transporter substrate-binding protein HisJ; Provisional


Pssm-ID: 185334 [Multi-domain]  Cd Length: 259  Bit Score: 45.41  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742   1 MKRFTATLTLIILLAGCRQPVVDEAQvtpavneakELRVGT--LYGPqIYVSSTQGS-AGFDYEMAARFAD-------FL 70
Cdd:PRK15437    1 MKKLVLSLSLVLAFSSATAAFAAIPQ---------NIRIGTdpTYAP-FESKNSQGElVGFDIDLAKELCKrintqctFV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  71 GKPLEmkpygninELYQALKQNEIDLIAAGLSDTRSRRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNALDAPVTVIADSS 150
Cdd:PRK15437   71 ENPLD--------ALIPSLKAKKIDAIMSSLSITEKRQQEIAFTDKLYAADSRLVVAKNSDIQPTVESLKGKRVGVLQGT 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 151 FVETLNrlkadnpNLEW-----QQVADKDNEELLSMIASGELSYTISDS---------TSININRRF-MPELRSgqvlEQ 215
Cdd:PRK15437  143 TQETFG-------NEHWapkgiEIVSYQGQDNIYSDLTAGRIDAAFQDEvaasegflkQPVGKDYKFgGPSVKD----EK 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1226745742 216 QQAVVWLLPPRGSDQLMSQLLRFWHQEQR-DGTLEHLVEKYF 256
Cdd:PRK15437  212 LFGVGTGMGLRKEDNELREALNKAFAEMRaDGTYEKLAKKYF 253
PBP2_TcyK cd13710
Substrate binding domain of an ABC transporter TcyJKLMN; the type 2 periplasmic binding ...
 35-257 8.62e-05

Substrate binding domain of an ABC transporter TcyJKLMN; the type 2 periplasmic binding protein fold; This group contains periplasmic cystine-binding domain (TcyK) of an ATP-binding cassette transporter from Bacillus subtilus and its closely related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270428 [Multi-domain]  Cd Length: 233  Bit Score: 43.82  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  35 KELRVGT--LYGPQIYVSSTQGSAGFDYE-MAARFADFLGKPLEMKPYGNINeLYQALKQNEIDLIAAGLSDTRSRRQQF 111
Cdd:cd13710     1 KTVKVATgaDTPPFSYEDKKGELTGYDIEvLKAIDKKLPQYKFKFKVTEFSS-ILTGLDSGKYDMAANNFSKTKERAKKF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 112 RLGPPLYRVNQVMVYragtpVPKD---LNALD-------APVTVIADSSFVETLNRLKADNP---NLEWQQVADKdneel 178
Cdd:cd13710    80 LFSKVPYGYSPLVLV-----VKKDsndINSLDdlagkttIVVAGTNYAKVLEAWNKKNPDNPikiKYSGEGINDR----- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 179 LSMIASGELSYTISDSTSIN-INRRFMPELRSGQVLEQQQAVVWLLPPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYFG 257
Cdd:cd13710   150 LKQVESGRYDALILDKFSVDtIIKTQGDNLKVVDLPPVKKPYVYFLFNKDQQKLQKDIDKALKELKKDGTLKKLSKKYFG 229
PBP2_YxeM cd13709
Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein ...
 35-257 8.68e-05

Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein fold; This group contains cystine-binding domain (YxeM) of a periplasmic receptor-dependent ATP-binding cassette transporter and its closely related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270427 [Multi-domain]  Cd Length: 227  Bit Score: 43.88  E-value: 8.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  35 KELRVGT--LYGPQIYVSSTQgSAGFDYEMAARFADFLGKPLEMKPyGNINELYQALKQNEIDLIAAGLSDTRSRRQQFR 112
Cdd:cd13709     1 KVIKVGSsgSSYPFTFKENGK-LKGFEVDVWNAIGKRTGYKVEFVT-ADFSGLFGMLDSGKVDTIANQITITPERQEKYD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 113 LGPP-LYRVNQVMVYRAGTPVpKDLNALDA-PVTVIADSSFVETLnrlKADNPNLEWQQVADKDNEELLSMIASGELSYT 190
Cdd:cd13709    79 FSEPyVYDGAQIVVKKDNNSI-KSLEDLKGkTVAVNLGSNYEKIL---KAVDKDNKITIKTYDDDEGALQDVALGRVDAY 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1226745742 191 ISDSTSI--NINRRFMPELRSGQVLEQQQAVVWLLPPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYFG 257
Cdd:cd13709   155 VNDRVSLlaKIKKRGLPLKLAGEPLVEEEIAFPFVKNEKGKKLLEKVNKALEEMRKDGTLKKISEKWFG 223
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 297-349 1.99e-04

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


Pssm-ID: 381596 [Multi-domain]  Cd Length: 59  Bit Score: 39.32  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1226745742 297 LAATSYQESHWNPRAR--SPTGVRGMMMLTLATAKQLG---VENRLDPEQSIRGGARY 349
Cdd:cd00442     2 LAAIIGQESGGNKPANagSGSGAAGLFQFMPGTWKAYGknsSSDLNDPEASIEAAAKY 59
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
 37-257 5.06e-04

Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic binding protein fold; This group contains cystine binding domain FliY and its related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270430 [Multi-domain]  Cd Length: 219  Bit Score: 41.60  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  37 LRVGT--LYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPyGNINELYQALKQNEIDLIAAGLSDTRSRRQQFRLG 114
Cdd:cd13712     2 LRIGLegTYPPFNFKDETGQLTGFEVDVAKALAAKLGVKPEFVT-TEWSGILAGLQAGKYDVIINQVGITPERQKKFDFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 115 PP-LYRVNQVMVYRAGTPVPKDLNALD-APVTVIADSSFVEtlnRLKADNPNLEWQQVadKDNEELLSMIASGELSYTIS 192
Cdd:cd13712    81 QPyTYSGIQLIVRKNDTRTFKSLADLKgKKVGVGLGTNYEQ---WLKSNVPGIDVRTY--PGDPEKLQDLAAGRIDAALN 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1226745742 193 DSTSININRRFMPELR-SGQVLEQQQAVVWLlpPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYFG 257
Cdd:cd13712   156 DRLAANYLVKTSLELPpTGGAFARQKSGIPF--RKGNPKLKAAINKAIEDLRADGTLAKLSEKWFG 219
PBP2_SMa0082_like cd01072
The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic ...
 33-148 5.79e-04

The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Sinorhizobium meliloti and its related proteins. The putative SMa0082-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270233 [Multi-domain]  Cd Length: 238  Bit Score: 41.48  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  33 EAKELRVGTLYG--PQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGNINELyQALKQNEIDLIAAGLSDTRSRRQQ 110
Cdd:cd01072    11 KRGKLKVGVLVDapPFGFVDASMQPQGYDVDVAKLLAKDLGVKLELVPVTGANRI-PYLQTGKVDMLIASLGITPERAKV 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1226745742 111 FRLGPPlYRVNQVMVYraGTPvpkdlnalDAPVTVIAD 148
Cdd:cd01072    90 VDFSQP-YAAFYLGVY--GPK--------DAKVKSPAD 116
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
 37-172 6.30e-04

Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold; This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 41.14  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  37 LRVGTLYG--PQIYVSSTQGSAGFDYEMAARFA-DFLGKPLEMK--PYGNINELyQALKQNEIDLIAAGLSDTRSRRQQF 111
Cdd:cd01000    10 LIVGVKPDlpPFGARDANGKIQGFDVDVAKALAkDLLGDPVKVKfvPVTSANRI-PALQSGKVDLIIATMTITPERAKEV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1226745742 112 RLGPPLYRVNQVMVYRAGTPVpKDLNALDAPVTVIADSSFVETLNRLKAdnPNLEWQQVAD 172
Cdd:cd01000    89 DFSVPYYADGQGLLVRKDSKI-KSLEDLKGKTILVLQGSTAEAALRKAA--PEAQLLEFDD 146
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
 34-136 7.74e-04

Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 periplasmic binding protein fold; This subgroup includes the periplasmic binding component of ABC transporter involved in uptake of mimosine MidA and its similar proteins. This periplasmic binding domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270225 [Multi-domain]  Cd Length: 230  Bit Score: 41.07  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  34 AKELRVGT--LYGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYGnINELYQALKQNEIDLIAAGLSDTRSRRQQF 111
Cdd:cd01004     1 AGTLTVGTnpTYPPYEFVDEDGKLIGFDVDLAKAIAKRLGLKVEIVNVS-FDGLIPALQSGRYDIIMSGITDTPERAKQV 79

                          90       100
                  ....*....|....*....|....*....
gi 1226745742 112 RLGPPLYRVNQVMVyRAGTPV----PKDL 136
Cdd:cd01004    80 DFVDYMKDGLGVLV-AKGNPKkiksPEDL 107
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
 30-172 8.31e-04

Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein fold; This subfamily comprises of the periplasmic-binding protein component of ABC transporter specific for cysteine and its closely related proteins. The cysteine-binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270412 [Multi-domain]  Cd Length: 229  Bit Score: 40.80  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  30 AVNEAKELRVGtLYG---PQIYVSSTQGSAGFDYEMAARFA-DFLGKPLEMKPYG-NINELYQALKQNEIDLIAAGLSDT 104
Cdd:cd13694     3 QIKQSGVIRIG-VFGdkpPFGYVDENGKFQGFDIDLAKQIAkDLFGSGVKVEFVLvEAANRVPYLTSGKVDLILANFTVT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1226745742 105 RSRRQQFRLGPPLYRVNQVMVYRAGTPVPKDLNALDAPVTVIADSSfveTLNRLKADNPN---LEWQQVAD 172
Cdd:cd13694    82 PERAEVVDFANPYMKVALGVVSPKDSNITSVAQLDGKTLLVNKGTT---AEKYFTKNHPEiklLKYDQNAE 149
PBP2_AatB_like cd00996
Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong ...
 57-165 1.73e-03

Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong to the type 2 periplasmic binding fold protein superfamily; This subfamily includes periplasmic binding domain of ATP-binding cassette transporter-like systems that serve as initial receptors in the ABC transport of amino acids and their derivatives in eubacteria. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The Abp proteins belong to the PBPI superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270217 [Multi-domain]  Cd Length: 227  Bit Score: 39.87  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  57 GFDYEMAARFADFLGKPLEMKPY---GNINElyqaLKQNEIDLIAAGLSDTRSRRQQFRLGPPlYRVN-QVMVYRAGTPV 132
Cdd:cd00996    28 GFDIDLAKEVAKRLGVEVEFQPIdwdMKETE----LNSGNIDLIWNGLTITDERKKKVAFSKP-YLENrQIIVVKKDSPI 102

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1226745742 133 --PKDLNalDAPVTVIADSSFVETLNRlkadNPNL 165
Cdd:cd00996   103 nsKADLK--GKTVGVQSGSSGEDALNA----DPNL 131
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
 34-256 4.33e-03

Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and related proteins; the type 2 periplasmic-binding protein fold; This family comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270222 [Multi-domain]  Cd Length: 228  Bit Score: 38.81  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742  34 AKELRVGTL--YGPQIYVSSTQGSAGFDYEMAARFADFLGKPLEMKPYgNINELYQALKQNEIDLIAAGLSDTRSRRQQF 111
Cdd:cd01001     1 ADTLRIGTEgdYPPFNFLDADGKLVGFDIDLANALCKRMKVKCEIVTQ-PWDGLIPALKAGKYDAIIASMSITDKRRQQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226745742 112 RLGPPLYR-VNQVMVYRAGTPVPKDLNALDAPVTVIADSSFVETLnrLKADNPNLEWqqVADKDNEELLSMIASGELSYT 190
Cdd:cd01001    80 DFTDPYYRtPSRFVARKDSPITDTTPAKLKGKRVGVQAGTTHEAY--LRDRFPEADL--VEYDTPEEAYKDLAAGRLDAV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1226745742 191 ISDSTSI-------NINR--RFMPELRSGQVLEQQQAVVWLlpPRGSDQLMSQLLRFWHQEQRDGTLEHLVEKYF 256
Cdd:cd01001   156 FGDKVALsewlkktKSGGccKFVGPAVPDPKYFGDGVGIAV--RKDDDALRAKLDKALAALKADGTYAEISKKYF 228
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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