NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|84375517|gb|EAP92420|]
View 

ABC-type sugar transport system, periplasmic component [Vibrio splendidus 12B01]

Protein Classification

type 2 periplasmic-binding domain-containing protein( domain architecture ID 229383)

type 2 periplasmic-binding protein (PBP2) is typically comprised of two globular subdomains connected by a flexible hinge; it binds its ligand in the cleft between these domains in a manner resembling a Venus flytrap; similar to the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 3-430 7.82e-128

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.


The actual alignment was detected with superfamily member PRK10974:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 438  Bit Score: 376.45  E-value: 7.82e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517    3 KLILAGVLSATAAMPAFATTQVTWWHAMGGQLGETVNKIATDFNASQDDYKITPIYKGSYTETLTAGIAAYRAGEAPNIL 82
Cdd:PRK10974   7 STALGLALGLALSGNAQAVTEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGNAPAIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   83 QVFDAGAATIMNAKGVaKPVQDILVESGYNFNSNDYLAGVRNFYADNQ-GKMVGMPFNSSTPVLYYNKDLLAEVGAD--- 158
Cdd:PRK10974  87 QVYEVGTATMMASKAI-KPVYDVFKDAGIPFDESQFVPTVAGYYSDAKtGHLLSQPFNSSTPVLYYNKDAFKKAGLDpeq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  159 APKTYEELEVVAKKLKAEG-HIAFSQSLTPWIMFENFKSRHNLPVSDQNNGYDGLSTKIMFNTKDMMMHVSKMKEWSVLG 237
Cdd:PRK10974 166 PPKTWQDLAAYAAKLRAAGmKCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEEMNKKG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  238 YYKYYGSDwDANQTPFERQEVAMWMGSSGSFGGLRNRVPFELGTTYLPYWKSVNPDAGLTFIGGAALFALNGHDQQQDKG 317
Cdd:PRK10974 246 DFTYVGRK-DESTEKFYNGDCAITTASSGSLANIRKYAKFNYGVGMMPYDADVKGAPQNAIIGGASLWVMQGKDKETYKG 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  318 VAAFFDYLTKPETQVYWHKTTGYVPVTTAAYELAKESGYYKEQPDAEVGVKQLSLKSG-EWTKGYRLGYYPQIREVMHRE 396
Cdd:PRK10974 325 VAKFLDFLAKPENAAEWHQKTGYLPITTAAYDLTREQGFYEKNPGADTATRQMLNKPPlPFTKGLRLGNMPQIRTIVDEE 404

                        410       420       430
                 ....*....|....*....|....*....|....
gi 84375517  397 FDNIFAGRSSVENSLDKVEDESSKLLKRFARTMN 430
Cdd:PRK10974 405 LESVWTGKKTPQQALDSAVERGNQLLRRFEKSTK 438
 
Name Accession Description Interval E-value
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
3-430 7.82e-128

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 376.45  E-value: 7.82e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517    3 KLILAGVLSATAAMPAFATTQVTWWHAMGGQLGETVNKIATDFNASQDDYKITPIYKGSYTETLTAGIAAYRAGEAPNIL 82
Cdd:PRK10974   7 STALGLALGLALSGNAQAVTEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGNAPAIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   83 QVFDAGAATIMNAKGVaKPVQDILVESGYNFNSNDYLAGVRNFYADNQ-GKMVGMPFNSSTPVLYYNKDLLAEVGAD--- 158
Cdd:PRK10974  87 QVYEVGTATMMASKAI-KPVYDVFKDAGIPFDESQFVPTVAGYYSDAKtGHLLSQPFNSSTPVLYYNKDAFKKAGLDpeq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  159 APKTYEELEVVAKKLKAEG-HIAFSQSLTPWIMFENFKSRHNLPVSDQNNGYDGLSTKIMFNTKDMMMHVSKMKEWSVLG 237
Cdd:PRK10974 166 PPKTWQDLAAYAAKLRAAGmKCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEEMNKKG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  238 YYKYYGSDwDANQTPFERQEVAMWMGSSGSFGGLRNRVPFELGTTYLPYWKSVNPDAGLTFIGGAALFALNGHDQQQDKG 317
Cdd:PRK10974 246 DFTYVGRK-DESTEKFYNGDCAITTASSGSLANIRKYAKFNYGVGMMPYDADVKGAPQNAIIGGASLWVMQGKDKETYKG 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  318 VAAFFDYLTKPETQVYWHKTTGYVPVTTAAYELAKESGYYKEQPDAEVGVKQLSLKSG-EWTKGYRLGYYPQIREVMHRE 396
Cdd:PRK10974 325 VAKFLDFLAKPENAAEWHQKTGYLPITTAAYDLTREQGFYEKNPGADTATRQMLNKPPlPFTKGLRLGNMPQIRTIVDEE 404

                        410       420       430
                 ....*....|....*....|....*....|....
gi 84375517  397 FDNIFAGRSSVENSLDKVEDESSKLLKRFARTMN 430
Cdd:PRK10974 405 LESVWTGKKTPQQALDSAVERGNQLLRRFEKSTK 438
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 23-417 2.11e-79

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 250.29  E-value: 2.11e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  23 QVTWWHAMGGQLGETVNKIATDFNASQDDYKITPIYKGSYTETLTAGIAAYRAGEAPNILQVFDAGAATIMnAKGVAKPV 102
Cdd:cd14748   1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLA-DSGALEPL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 103 QDILVESGYNFnsNDYLAGVRNfYADNQGKMVGMPFNSSTPVLYYNKDLLAEVGAD---APKTYEELEVVAKKLKAEGH- 178
Cdd:cd14748  80 DDYIDKDGVDD--DDFYPAALD-AGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDpekPPKTWDELEEAAKKLKDKGGk 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 179 -----IAFSQSLTPWiMFENFKSrhnlpvsdQNNG--YDGLSTKIMFNTKDMMMHVSKMKEWSVLGYYKYYGSDWDANQt 251
Cdd:cd14748 157 tgrygFALPPGDGGW-TFQALLW--------QNGGdlLDEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQD- 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 252 PFERQEVAMWMGSSGSFGGLRNRVP-FELGTTYLPYWKSVNPDaglTFIGGAALFALNGHDQQQdKGVAAFFDYLTKPET 330
Cdd:cd14748 227 AFISGKVAMTINGTWSLAGIRDKGAgFEYGVAPLPAGKGKKGA---TPAGGASLVIPKGSSKKK-EAAWEFIKFLTSPEN 302

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 331 QVYWHKTTGYVPVTTAAYElaKESGYYKEQPDAEVGVKQLSLKSGEwtkGYRLGYYPQIREVMHREFDNIFAGRSSVENS 410
Cdd:cd14748 303 QAKWAKATGYLPVRKSAAE--DPEEFLAENPNYKVAVDQLDYAKPW---GPPVPNGAEIRDELNEALEAALLGKKTPEEA 377


                ....*..
gi 84375517 411 LDKVEDE 417
Cdd:cd14748 378 LKEAQEK 384
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-334 1.17e-52

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 180.24  E-value: 1.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   1 MNKLILAGVLSATAAM-----------PAFATTQVTWWHaMGGQLGETVNKIATDFNASQDDYKITPIYKGsYTETLTAG 69
Cdd:COG1653   1 MRRLALALAAALALALaacggggsgaaAAAGKVTLTVWH-TGGGEAAALEALIKEFEAEHPGIKVEVESVP-YDDYRTKL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  70 IAAYRAGEAPNILQVFDAGAATIMnAKGVAKPVQDILveSGYNFNSNDYLAGVRNFYADNqGKMVGMPFNSSTPVLYYNK 149
Cdd:COG1653  79 LTALAAGNAPDVVQVDSGWLAEFA-AAGALVPLDDLL--DDDGLDKDDFLPGALDAGTYD-GKLYGVPFNTDTLGLYYNK 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 150 DLLAEVGADAPKTYEELEVVAKKLKAE-GHIAFSQSLTPWIMFENFKSRHNLPVSDQNngydglsTKIMFNTKDMMMHVS 228
Cdd:COG1653 155 DLFEKAGLDPPKTWDELLAAAKKLKAKdGVYGFALGGKDGAAWLDLLLSAGGDLYDED-------GKPAFDSPEAVEALE 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 229 KMKEWSVLGY--YKYYGSDWDANQTPFERQEVAMWMGSSGSFGGLRNRVP-FELGTTYLPYWKSVNPDAglTFIGGAALF 305
Cdd:COG1653 228 FLKDLVKDGYvpPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPdFDVGVAPLPGGPGGKKPA--SVLGGSGLA 305

                       330       340
                ....*....|....*....|....*....
gi 84375517 306 ALNGHDQQqdKGVAAFFDYLTKPETQVYW 334
Cdd:COG1653 306 IPKGSKNP--EAAWKFLKFLTSPEAQAKW 332
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 40-352 2.44e-21

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 93.24  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517    40 KIATDFNASQDdYKITPIYKGS--YTETLTAGIAAyraGEAPNI-LQVFDAGAATIMNAKGVAKPVQDIlvesgynfnsn 116
Cdd:pfam13416   1 ALAKAFEKKTG-VTVEVEPQASndLQAKLLAAAAA---GNAPDLdVVWIAADQLATLAEAGLLADLSDV----------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   117 DYLAGVRNFYADNQ--GKMVGMPFNSSTP-VLYYNKDLLAEVGADaPKTYEELEVVAKKLKAeghiAFSQSLTPWIMFEN 193
Cdd:pfam13416  66 DNLDDLPDALDAAGydGKLYGVPYAASTPtVLYYNKDLLKKAGED-PKTWDELLAAAAKLKG----KTGLTDPATGWLLW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   194 FKSRHNLPVSDQNNGYDGLstkimfntKDMMMHVSKMKEWSvlgyyKYYGSDWDANQtPFERQEVAMWMGSSGSFGGLRN 273
Cdd:pfam13416 141 ALLADGVDLTDDGKGVEAL--------DEALAYLKKLKDNG-----KVYNTGADAVQ-LFANGEVAMTVNGTWAAAAAKK 206

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84375517   274 RvPFELGTTYlpywksvnPDAGlTFIGGAAlFALNGHDQQQDKGVAAFFDYLTKPETQVYWHKTTGYVPVTTAAYELAK 352
Cdd:pfam13416 207 A-GKKLGAVV--------PKDG-SFLGGKG-LVVPAGAKDPRLAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDE 274
 
Name Accession Description Interval E-value
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
3-430 7.82e-128

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 376.45  E-value: 7.82e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517    3 KLILAGVLSATAAMPAFATTQVTWWHAMGGQLGETVNKIATDFNASQDDYKITPIYKGSYTETLTAGIAAYRAGEAPNIL 82
Cdd:PRK10974   7 STALGLALGLALSGNAQAVTEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGNAPAIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   83 QVFDAGAATIMNAKGVaKPVQDILVESGYNFNSNDYLAGVRNFYADNQ-GKMVGMPFNSSTPVLYYNKDLLAEVGAD--- 158
Cdd:PRK10974  87 QVYEVGTATMMASKAI-KPVYDVFKDAGIPFDESQFVPTVAGYYSDAKtGHLLSQPFNSSTPVLYYNKDAFKKAGLDpeq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  159 APKTYEELEVVAKKLKAEG-HIAFSQSLTPWIMFENFKSRHNLPVSDQNNGYDGLSTKIMFNTKDMMMHVSKMKEWSVLG 237
Cdd:PRK10974 166 PPKTWQDLAAYAAKLRAAGmKCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEEMNKKG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  238 YYKYYGSDwDANQTPFERQEVAMWMGSSGSFGGLRNRVPFELGTTYLPYWKSVNPDAGLTFIGGAALFALNGHDQQQDKG 317
Cdd:PRK10974 246 DFTYVGRK-DESTEKFYNGDCAITTASSGSLANIRKYAKFNYGVGMMPYDADVKGAPQNAIIGGASLWVMQGKDKETYKG 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  318 VAAFFDYLTKPETQVYWHKTTGYVPVTTAAYELAKESGYYKEQPDAEVGVKQLSLKSG-EWTKGYRLGYYPQIREVMHRE 396
Cdd:PRK10974 325 VAKFLDFLAKPENAAEWHQKTGYLPITTAAYDLTREQGFYEKNPGADTATRQMLNKPPlPFTKGLRLGNMPQIRTIVDEE 404

                        410       420       430
                 ....*....|....*....|....*....|....
gi 84375517  397 FDNIFAGRSSVENSLDKVEDESSKLLKRFARTMN 430
Cdd:PRK10974 405 LESVWTGKKTPQQALDSAVERGNQLLRRFEKSTK 438
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 23-417 2.11e-79

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 250.29  E-value: 2.11e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  23 QVTWWHAMGGQLGETVNKIATDFNASQDDYKITPIYKGSYTETLTAGIAAYRAGEAPNILQVFDAGAATIMnAKGVAKPV 102
Cdd:cd14748   1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLA-DSGALEPL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 103 QDILVESGYNFnsNDYLAGVRNfYADNQGKMVGMPFNSSTPVLYYNKDLLAEVGAD---APKTYEELEVVAKKLKAEGH- 178
Cdd:cd14748  80 DDYIDKDGVDD--DDFYPAALD-AGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDpekPPKTWDELEEAAKKLKDKGGk 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 179 -----IAFSQSLTPWiMFENFKSrhnlpvsdQNNG--YDGLSTKIMFNTKDMMMHVSKMKEWSVLGYYKYYGSDWDANQt 251
Cdd:cd14748 157 tgrygFALPPGDGGW-TFQALLW--------QNGGdlLDEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQD- 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 252 PFERQEVAMWMGSSGSFGGLRNRVP-FELGTTYLPYWKSVNPDaglTFIGGAALFALNGHDQQQdKGVAAFFDYLTKPET 330
Cdd:cd14748 227 AFISGKVAMTINGTWSLAGIRDKGAgFEYGVAPLPAGKGKKGA---TPAGGASLVIPKGSSKKK-EAAWEFIKFLTSPEN 302

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 331 QVYWHKTTGYVPVTTAAYElaKESGYYKEQPDAEVGVKQLSLKSGEwtkGYRLGYYPQIREVMHREFDNIFAGRSSVENS 410
Cdd:cd14748 303 QAKWAKATGYLPVRKSAAE--DPEEFLAENPNYKVAVDQLDYAKPW---GPPVPNGAEIRDELNEALEAALLGKKTPEEA 377


                ....*..
gi 84375517 411 LDKVEDE 417
Cdd:cd14748 378 LKEAQEK 384
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-334 1.17e-52

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 180.24  E-value: 1.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   1 MNKLILAGVLSATAAM-----------PAFATTQVTWWHaMGGQLGETVNKIATDFNASQDDYKITPIYKGsYTETLTAG 69
Cdd:COG1653   1 MRRLALALAAALALALaacggggsgaaAAAGKVTLTVWH-TGGGEAAALEALIKEFEAEHPGIKVEVESVP-YDDYRTKL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  70 IAAYRAGEAPNILQVFDAGAATIMnAKGVAKPVQDILveSGYNFNSNDYLAGVRNFYADNqGKMVGMPFNSSTPVLYYNK 149
Cdd:COG1653  79 LTALAAGNAPDVVQVDSGWLAEFA-AAGALVPLDDLL--DDDGLDKDDFLPGALDAGTYD-GKLYGVPFNTDTLGLYYNK 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 150 DLLAEVGADAPKTYEELEVVAKKLKAE-GHIAFSQSLTPWIMFENFKSRHNLPVSDQNngydglsTKIMFNTKDMMMHVS 228
Cdd:COG1653 155 DLFEKAGLDPPKTWDELLAAAKKLKAKdGVYGFALGGKDGAAWLDLLLSAGGDLYDED-------GKPAFDSPEAVEALE 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 229 KMKEWSVLGY--YKYYGSDWDANQTPFERQEVAMWMGSSGSFGGLRNRVP-FELGTTYLPYWKSVNPDAglTFIGGAALF 305
Cdd:COG1653 228 FLKDLVKDGYvpPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPdFDVGVAPLPGGPGGKKPA--SVLGGSGLA 305

                       330       340
                ....*....|....*....|....*....
gi 84375517 306 ALNGHDQQqdKGVAAFFDYLTKPETQVYW 334
Cdd:COG1653 306 IPKGSKNP--EAAWKFLKFLTSPEAQAKW 332
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 24-417 6.33e-28

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 114.04  E-value: 6.33e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  24 VTWWHAMGGQLGETVNKIATDFNASQDDYKI--TPIYKGSYTETLTAGIAAyraGEAPNILQVFDAGAATiMNAKGVAKP 101
Cdd:cd13585   2 LTFWDWGQPAETAALKKLIDAFEKENPGVKVevVPVPYDDYWTKLTTAAAA---GTAPDVFYVDGPWVPE-FASNGALLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 102 VQDILVESGYNFNSNDYLAGVRNFyadnQGKMVGMPFNSSTPVLYYNKDLLAEVGA--DAPKTYEELEVVAKKLKAEGH- 178
Cdd:cd13585  78 LDDYIEKDGLDDDFPPGLLDAGTY----DGKLYGLPFDADTLVLFYNKDLFDKAGPgpKPPWTWDELLEAAKKLTDKKGg 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 179 ---IAFSQSLTPWIMFENFksrhnlpvSDQNNG--YDGLSTKIMFNTKDMMMHVSKMKEWsvlgYYKYY-----GSDWDA 248
Cdd:cd13585 154 qygFALRGGSGGQTQWYPF--------LWSNGGdlLDEDDGKATLNSPEAVEALQFYVDL----YKDGVapssaTTGGDE 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 249 NQTPFERQEVAMWMGSSGSFGGLRNR-VPFELGTTYLPYWKSVNPdagLTFIGGAAlFALNGHDQQQDkGVAAFFDYLTK 327
Cdd:cd13585 222 AVDLFASGKVAMMIDGPWALGTLKDSkVKFKWGVAPLPAGPGGKR---ASVLGGWG-LAISKNSKHPE-AAWKFIKFLTS 296

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 328 PETQVYWHKTTGYVPVTTAAYElakesgYYKEQPDAEVGVKQLSLKSGEWTKGYRLGYYPQIREVMHREFDNIFAG--RS 405
Cdd:cd13585 297 KENQLKLGGAAGPAALAAAAAS------AAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGK 370

                       410
                ....*....|..
gi 84375517 406 SVENSLDKVEDE 417
Cdd:cd13585 371 SPEEALKEAAKE 382
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 36-416 4.99e-26

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 108.62  E-value: 4.99e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  36 ETVNKIATDFNASQDDYKI--TPIYKGSYTETLTAGIAAyraGEAPNILQVFDAGAATIMNAKGVAKPVQDILVESGYNf 113
Cdd:cd14749  15 KYMDELIADFEKENPNIKVkvVVFPYDNYKTKLKTAVAA---GEGPDVFNLWPGGWLAEFVKAGLLLPLTDYLDPNGVD- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 114 nsNDYLAGvrnfYADN---QGKMVGMPFNSSTPVLYYNKDLLAEVGAD-APKTYEELEVVAKKLK--AEGHIAFSQSL-- 185
Cdd:cd14749  91 --KRFLPG----LADAvtfNGKVYGIPFAARALALFYNKDLFEEAGGVkPPKTWDELIEAAKKDKfkAKGQTGFGLLLga 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 186 TPWIMFENFKSRHNLPVSDQNNGYDGLStkimFNTKDMMMHVSKMKEWSVLGY--YKYYGSDWDANQTPFERQEVAMWMG 263
Cdd:cd14749 165 QGGHWYFQYLVRQAGGGPLSDDGSGKAT----FNDPAFVQALQKLQDLVKAGAfqEGFEGIDYDDAGQAFAQGKAAMNIG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 264 SSGSFGGLRNRVP-FELGTTYLPywkSVNPDAGLTFIGGAAL-FALNGHDQQQDKgVAAFFDYLTKPETQVYWHKTTGYV 341
Cdd:cd14749 241 GSWDLGAIKAGEPgGKIGVFPFP---TVGKGAQTSTIGGSDWaIAISANGKKKEA-AVKFLKYLTSPEVMKQYLEDVGLL 316

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84375517 342 PVTTAAYELAKESGYYKEQPDAEVGVKQLSLKSGEWtkgyrlgYYPQIREVMHREFDNIFAGRSSVENSLDKVED 416
Cdd:cd14749 317 PAKEVVAKDEDPDPVAILGPFADVLNAAGSTPFLDE-------YWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQS 384
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
4-423 1.29e-23

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 101.95  E-value: 1.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   4 LILAGVLSA--------TAAMPAFATTQVTWWHamGGQLGETVNKIATDFNAsQDDYKITPIYKGsYTETLTAGIAAYRA 75
Cdd:COG2182  13 LALALALAAcgsgssssGSSSAAGAGGTLTVWV--DDDEAEALEEAAAAFEE-EPGIKVKVVEVP-WDDLREKLTTAAPA 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  76 GEAPNILQVFDAGAATIMNAkGVAKPVQDILVESgynfnsNDYL-AGVRNFYADnqGKMVGMPFNSSTPVLYYNKDLLAE 154
Cdd:COG2182  89 GKGPDVFVGAHDWLGELAEA-GLLAPLDDDLADK------DDFLpAALDAVTYD--GKLYGVPYAVETLALYYNKDLVKA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 155 vgaDAPKTYEELEVVAKKLKAEGHIAFsqsltpwiMFENFKSRHNLPVSDQNNGY-----DGLSTKIMFNTKDMMMHVSK 229
Cdd:COG2182 160 ---EPPKTWDELIAAAKKLTAAGKYGL--------AYDAGDAYYFYPFLAAFGGYlfgkdGDDPKDVGLNSPGAVAALEY 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 230 MKEWSVLGYYKyYGSDWDANQTPFERQEVAMWMGSSGSFGGLRNRVPFELGTTYLPywKSVNPDAGLTFIGGAAlFALNG 309
Cdd:COG2182 229 LKDLIKDGVLP-ADADYDAADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLP--TLAGGKPAKPFVGVKG-FGVSA 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 310 HDQQQDkGVAAFFDYLTKPETQVYWHKTTGYVPVTTAAYELAKesgyYKEQPDAEVGVKQlsLKSGEwtkgyrlgYYPQI 389
Cdd:COG2182 305 YSKNKE-AAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAE----VKADPLIAAFAEQ--AEYAV--------PMPNI 369

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 84375517 390 REV------MHREFDNIFAGRSSVENSLDKVEDESSKLLK 423
Cdd:COG2182 370 PEMgavwtpLGTALQAIASGKADPAEALDAAQKQIEAAIA 409
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 40-352 2.44e-21

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 93.24  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517    40 KIATDFNASQDdYKITPIYKGS--YTETLTAGIAAyraGEAPNI-LQVFDAGAATIMNAKGVAKPVQDIlvesgynfnsn 116
Cdd:pfam13416   1 ALAKAFEKKTG-VTVEVEPQASndLQAKLLAAAAA---GNAPDLdVVWIAADQLATLAEAGLLADLSDV----------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   117 DYLAGVRNFYADNQ--GKMVGMPFNSSTP-VLYYNKDLLAEVGADaPKTYEELEVVAKKLKAeghiAFSQSLTPWIMFEN 193
Cdd:pfam13416  66 DNLDDLPDALDAAGydGKLYGVPYAASTPtVLYYNKDLLKKAGED-PKTWDELLAAAAKLKG----KTGLTDPATGWLLW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   194 FKSRHNLPVSDQNNGYDGLstkimfntKDMMMHVSKMKEWSvlgyyKYYGSDWDANQtPFERQEVAMWMGSSGSFGGLRN 273
Cdd:pfam13416 141 ALLADGVDLTDDGKGVEAL--------DEALAYLKKLKDNG-----KVYNTGADAVQ-LFANGEVAMTVNGTWAAAAAKK 206

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84375517   274 RvPFELGTTYlpywksvnPDAGlTFIGGAAlFALNGHDQQQDKGVAAFFDYLTKPETQVYWHKTTGYVPVTTAAYELAK 352
Cdd:pfam13416 207 A-GKKLGAVV--------PKDG-SFLGGKG-LVVPAGAKDPRLAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDE 274
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 24-423 9.94e-19

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 87.37  E-value: 9.94e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  24 VTWWHAMGGQLGETVNKIATDFNASQDDYKITPIY---KGSYTETLTAgIAAyraGEAPNILQVFDAGAATIMNAkGVAK 100
Cdd:cd14747   2 LTVWAMGNSAEAELLKELADEFEKENPGIEVKVQVlpwGDAHTKITTA-AAS---GDGPDVVQLGNTWVAEFAAM-GALE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 101 PVQDILVESGynfNSNDYLAGVRNFYADNqGKMVGMPFNSSTPVLYYNKDLLAEVGAD-APKTYEELEVVAKKLKAEG-- 177
Cdd:cd14747  77 DLTPYLEDLG---GDKDLFPGLVDTGTVD-GKYYGVPWYADTRALFYRTDLLKKAGGDeAPKTWDELEAAAKKIKADGpd 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 178 HIAFS--------QSLTPWImfenFKSRHNLPVSDQNNG-------------YDGLSTKiMFNTKDMMMHVSkmkewsvl 236
Cdd:cd14747 153 VSGFAipgkndvwHNALPFV----WGAGGDLATKDKWKAtldspeavaglefYTSLYQK-GLSPKSTLENSA-------- 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 237 gyykyygsdwDANQTpFERQEVAMWMGSSGSFGGLRNRVP---FELGTTYLPywkSVNPDAGLTFIGGA--ALFAlnghD 311
Cdd:cd14747 220 ----------DVEQA-FANGKVAMIISGPWEIGAIREAGPdlaGKWGVAPLP---GGPGGGSPSFAGGSnlAVFK----G 281

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 312 QQQDKGVAAFFDYLTKPETQVYWHKTTGYVPVTTAAYELAKesgyYKEQPDAEVGVKQLSL-----KSGEWTkgyrlgyy 386
Cdd:cd14747 282 SKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSAWDDPS----LANDPLLAVFAEQLKTgkatpATPEWG-------- 349

                       410       420       430
                ....*....|....*....|....*....|....*...
gi 84375517 387 pQIREVMHREFDNIFAG-RSSVENSLDKVEDESSKLLK 423
Cdd:cd14747 350 -EIEAELVLVLEEVWIGvGADVEDALDKAAAEINEILN 386
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 35-331 8.46e-17

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 80.54  E-value: 8.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517    35 GETVNKIATDFNASQDDYKITPIYkGSYTETLTAGIAAYRAGEAPNILQVFDAGAATIMNAKGVAKPVQDILVESGYNFN 114
Cdd:pfam01547   7 AAALQALVKEFEKEHPGIKVEVES-VGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   115 SNDYlagvrnfyadnqgkmvGMPFNSSTPVLYYNKDLLAEVGADAPKTYEELEVVAKKLKAEG-----HIAFSQSLTPWI 189
Cdd:pfam01547  86 PKLY----------------GVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGkspggAGGGDASGTLGY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   190 MFENFKSRHNLPVSDQNNGyDGLSTKIMFNTKDMMMHVSKMKEWSVLGYYKYYGSDWDANQTPFERQEVAMWMGSSGS-- 267
Cdd:pfam01547 150 FTLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAal 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84375517   268 -FGGLRNRVPFELGTTYLPYWKSVNP-DAGLTFIGGAALFALNgHDQQQDKGVAAFFDYLTKPETQ 331
Cdd:pfam01547 229 aANKVKLKVAFAAPAPDPKGDVGYAPlPAGKGGKGGGYGLAIP-KGSKNKEAAKKFLDFLTSPEAQ 293
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 24-417 5.93e-16

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 78.88  E-value: 5.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  24 VTWWHAMGGQLGETVNKIATDFNASQDDYKITPIY-KGSYTETLTAGIAAYRAG-EAPNILQV------FDAGAatimna 95
Cdd:cd14750   2 ITFAAGSDGQEGELLKKAIAAFEKKHPDIKVEIEElPASSDDQRQQLVTALAAGsSAPDVLGLdviwipEFAEA------ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  96 kGVAKPVQDILVESGynfnSNDYLAGVR--NFYadnQGKMVGMPFNSSTPVLYYNKDLLAEVGADAPKTYEELEVVAKKL 173
Cdd:cd14750  76 -GWLLPLTEYLKEEE----DDDFLPATVeaNTY---DGKLYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 174 KAEGH--IAFsqsLTPWIMFE----NFksrhnLPVSDQNNG--YDGLSTKIMFNTKDMMMHVSKMKEW--------SVLG 237
Cdd:cd14750 148 KAGEPgiWGY---VFQGKQYEglvcNF-----LELLWSNGGdiFDDDSGKVTVDSPEALEALQFLRDLigegispkGVLT 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 238 yykyYGSDwDANQTpFERQEVAM---WMGSSGSFGGLRNRVPFELGTTYLPYWKSVNPDAGLtfiGGAALfALNGHDQQQ 314
Cdd:cd14750 220 ----YGEE-EARAA-FQAGKAAFmrnWPYAYALLQGPESAVAGKVGVAPLPAGPGGGSASTL---GGWNL-AISANSKHK 289

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 315 DkGVAAFFDYLTKPETQVYWHKTTGYVPVTTAAYelaKESGYYKEQPDAEVGVKQLslksgEWTKGY-RLGYYPQIREVM 393
Cdd:cd14750 290 E-AAWEFVKFLTSPEVQKRRAINGGLPPTRRALY---DDPEVLEAYPFLPALLEAL-----ENAVPRpVTPKYPEVSTAI 360

                       410       420
                ....*....|....*....|....
gi 84375517 394 HREFDNIFAGRSSVENSLDKVEDE 417
Cdd:cd14750 361 QIALSAALSGQATPEEALKQAQEK 384
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 24-417 1.88e-15

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 77.42  E-value: 1.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  24 VTWWHAMGGQLGETVNKIATDFNASQDDYKITPIyKGSYTETLTAGIAAYRAGEAPNILQVFDAGAATIMNAkGVAKPVq 103
Cdd:cd14751   2 ITFWHTSSDEEKVLYEKLIPAFEKEYPKIKVKAV-RVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKL-GYLQPL- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 104 DILVESgynFNSNDYLAGV--RNFYadnQGKMVGMPFNSSTPVLYYNKDLLAEVGADAPKTYEEL-EVVAKKLKAEGHIA 180
Cdd:cd14751  79 DGTPAF---DDIVDYLPGPmeTNRY---NGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELvAAAKAIKKKKGRYG 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 181 FSQS-LTPWIMFENFKSRHNLPVSDQNngydglsTKIMFNTKDMMMHVSKMKEWSVLGYYKYYGSDWDAN-QTPFERQEV 258
Cdd:cd14751 153 LYISgDGPYWLLPFLWSFGGDLTDEKK-------ATGYLNSPESVRALETIVDLYDEGAITPCASGGYPNmQDGFKSGRY 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 259 AM-----WMgSSGSFGGLRNRVPFELGTTYLPywksVNPDAGLTFIGGAALFALNGHDQQqdKGVAAFFDYLTKPETQVY 333
Cdd:cd14751 226 AMivngpWA-YADILGGKEFKDPDNLGIAPVP----AGPGGSGSPVGGEDLVIFKGSKNK--DAAWKFVKFMSSAEAQAL 298

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 334 WHKTTGYVPVTTAAYELAKESGyykeqpDAEVGVKQLSLKSG-------EWTKgyrlgyypqIREVMHREFDNIFAGRSS 406
Cdd:cd14751 299 TAAKLGLLPTRTSAYESPEVAN------NPMVAAFKPALETAvprppipEWGE---------LFEPLTLAFAKVLRGEKS 363

                       410
                ....*....|.
gi 84375517 407 VENSLDKVEDE 417
Cdd:cd14751 364 PREALDEAAKQ 374
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 24-417 3.41e-13

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 70.40  E-value: 3.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  24 VTWWHAMGGQLgETVNKIATDFNAsQDDYKITPIYKGSyTETLTAGIAAYRAGEAPNILQV-FDAGAAtiMNAKGVAKPV 102
Cdd:cd13586   2 ITVWTDEDGEL-EYLKELAEEFEK-KYGIKVEVVYVDS-GDTREKFITAGPAGKGPDVFFGpHDWLGE--LAAAGLLAPI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 103 QDILVESgyNFNSNDYLAGVRnfYadnQGKMVGMPFNSSTPVLYYNKDLLAEVgadaPKTYEELEVVAKKLKAEghiafS 182
Cdd:cd13586  77 PEYLAVK--IKNLPVALAAVT--Y---NGKLYGVPVSVETIALFYNKDLVPEP----PKTWEELIALAKKFNDK-----A 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 183 QSLTPWIMfenfksrhnlpvsDQNNGY-----------------DGLSTKIMFNTKDMMMHVSKMKEWSVLGYYKYYGSD 245
Cdd:cd13586 141 GGKYGFAY-------------DQTNPYfsypflaafggyvfgenGGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLD 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 246 WDANQTPFERQEVAMWMGSSGSFGGLRNRvPFELGTTYLPywKSVNPDAGLTFIGGAAlFALNGHDQQQDKGVaAFFDYL 325
Cdd:cd13586 208 YDIADALFKEGKAAMIINGPWDLADYKDA-GINFGVAPLP--TLPGGKQAAPFVGVQG-AFVSAYSKNKEAAV-EFAEYL 282

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 326 TKPETQVYWHKTTGYVPVTTAAYELAKEsgyyKEQPDAEVGVKQLSlksgewtKGYRLGYYPQIREV---MHREFDNIFA 402
Cdd:cd13586 283 TSDEAQLLLFEKTGRIPALKDALNDAAV----KNDPLVKAFAEQAQ-------YGVPMPNIPEMAAVwdaMGNALNLVAS 351

                       410
                ....*....|....*
gi 84375517 403 GRSSVENSLDKVEDE 417
Cdd:cd13586 352 GKATPEEAAKDAVAA 366
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 24-417 6.90e-13

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 69.75  E-value: 6.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  24 VTWWHAMGGQLGETVNKIATDFNASQDDYKITPIYKGsyTETLTAGI-AAYRAGEAPNI-LQVFDAGAATImnAKGVAKP 101
Cdd:cd13522   2 ITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQD--TEARRQFFsTAAAGGKGPDVvFGPSDSLGPFA--AAGLLAP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 102 VQDILVESgyNFNSNDYLAGVRNfyadnQGKMVGMPFNSSTPVLYYNKDLLAEvgaDAPKTYEELEVVAKKLKAEGHIAF 181
Cdd:cd13522  78 LDEYVSKS--GKYAPNTIAAMKL-----NGKLYGVPVSVGAHLMYYNKKLVPK---NPPKTWQELIALAQGLKAKNVWGL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 182 SQSLT------PWI------MFEnFKSRHNLPVSDQNNGYDGLstKIMFNTKDMMMHVSKmkewsvlgyykyyGSDWDAN 249
Cdd:cd13522 148 VYNQNepyffaAWIggfggqVFK-ANNGKNNPTLDTPGAVEAL--QFLVDLKSKYKIMPP-------------ETDYSIA 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 250 QTPFERQEVAMWMGSSGSFGGLRNRVPFELGTTYLPYWKsvNPDAGLTFIGGAAlFALNGHDQQQdKGVAAFFDYLTKPE 329
Cdd:cd13522 212 DALFKAGKAAMIINGPWDLGDYRQALKINLGVAPLPTFS--GTKHAAPFVGGKG-FGINKESQNK-AAAVEFVKYLTSYQ 287

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 330 TQVYWHKTTGYVPVTTAAYELA---KESGYYKEQPDAEVGVKQLSLKsgewtkgyrlgYYPQIREVMHREFDNIFAGRSS 406
Cdd:cd13522 288 AQLVLFDDAGDIPANLQAYESPavqNKPAQKASAEQAAYGVPMPNIP-----------EMRAVWDAFRIAVNSVLAGKVT 356

                       410
                ....*....|.
gi 84375517 407 VENSLDKVEDE 417
Cdd:cd13522 357 PEAAAKDAQQE 367
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 24-367 6.99e-10

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 60.47  E-value: 6.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  24 VTWWHAMGGQLGETVNKIATDFNA--SQDDYKITPIYKGSYTETLTAGIAAyraGEAPNILqVFDAGAATIMNAKGVAKP 101
Cdd:cd13657   2 ITIWHALTGAEEDALQQIIDEFEAkyPVPNVKVPFEKKPDLQNKLLTAIPA---GEGPDLF-IWAHDWIGQFAEAGLLVP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 102 VQDILVEsgynFNSNDYLAGVRNfYADNQGKMVGMPFNSSTPVLYYNKDLLAEVgadaPKTYEELEVVAKKL--KAEGHI 179
Cdd:cd13657  78 ISDYLSE----DDFENYLPTAVE-AVTYKGKVYGLPEAYETVALIYNKALVDQP----PETTDELLAIMKDHtdPAAGSY 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 180 AFSQSLT------PWImfenfksrhnlpvsdqnNGY-----DGLSTKIMFNTKDMMMHVSKMKEWSvlgyYKYYGSD--W 246
Cdd:cd13657 149 GLAYQVSdayfvsAWI-----------------FGFggyyfDDETDKPGLDTPETIKGIQFLKDFS----WPYMPSDpsY 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 247 DANQTPFERQEVAMWMGSSGSFGGLRNRVpFELGTTYLPYWKSVNPDAglTFIGGAALFALNGHDQQQDKGVAAFFDYLT 326
Cdd:cd13657 208 NTQTSLFNEGKAAMIINGPWFIGGIKAAG-IDLGVAPLPTVDGTNPPR--PYSGVEGIYVTKYAERKNKEAALDFAKFFT 284

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 84375517 327 KPETQVYWHKTTGYVPVTTAAYELAKESGY-----YKEQpdAEVGV 367
Cdd:cd13657 285 TAEASKILADENGYVPAATNAYDDAEVAADpviaaFKAQ--AEHGV 328
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 131-371 6.81e-09

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 57.11  E-value: 6.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 131 GKMVGMPFNSSTPVLYYNKDLLaevgADAPKTYEELEVVAKKL--KAEGHIAFsqsLTPWimfENFksRHNLPVSDQNNG 208
Cdd:cd13658  98 GKLYGLPAAVETLALYYNKDLV----KNAPKTFDELEALAKDLtkEKGKQYGF---LADA---TNF--YYSYGLLAGNGG 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 209 Y-------DGLSTKIMFNTKDMMMHVSKMKEWSVLGYYKyYGSDWDANQTPFERQEVAMWMGSSGSFGGLRNrVPFELGT 281
Cdd:cd13658 166 YifkkngsDLDINDIGLNSPGAVKAVKFLKKWYTEGYLP-KGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQE-AGVNYGV 243

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 282 TYLPYWKSVNPDAglTFIGGAA--LFALNGHDQQQDKgvaaFFDYLTKPETQVYWHKTTGYVPVTTAAYELAKEsgyyKE 359
Cdd:cd13658 244 APLPTLPNGKPMA--PFLGVKGwyLSAYSKHKEWAQK----FMEFLTSKENLKKRYDETNEIPPRKDVRSDPEI----KN 313

                       250
                ....*....|..
gi 84375517 360 QPDAEVGVKQLS 371
Cdd:cd13658 314 NPLTSAFAKQAS 325
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 21-174 1.19e-06

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 50.40  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  21 TTQVTWWHAMGGQLGETVNK------IATDFNAsqdDYKITPIYKGSYTETLTAGIAAyraGEAPNILQVFDaGAATIMN 94
Cdd:cd13580   2 PVTITIVANLGGNPKPDPDDnpytkyLEEKTNI---DVKVKWVPDSSYDEKLNLALAS---GDLPDIVVVND-PQLSITL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  95 AK-GVAKPVQDILVESGYNFNSNDYLAGVRNFYADnqGKMVGMPF---NSSTPVLYYNKDLLAEVGADAPKTYEELEVVA 170
Cdd:cd13580  75 VKqGALWDLTDYLDKYYPNLKKIIEQEGWDSASVD--GKIYGIPRkrpLIGRNGLWIRKDWLDKLGLEVPKTLDELYEVA 152


                ....
gi 84375517 171 KKLK 174
Cdd:cd13580 153 KAFT 156
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
131-177 2.91e-04

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 42.69  E-value: 2.91e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 84375517  131 GKMVGMPFNSSTPVLYYNKDLLAEvgadAPKTYEELEVVAKKLKAEG 177
Cdd:PRK09474 127 GKLIGYPIAVEALSLIYNKDLVPT----PPKTWEEIPALDKELKAKG 169
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 41-166 6.76e-04

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 41.46  E-value: 6.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  41 IATDFNAsQDDYKITPIYKGsyTETLTAGIAAYRAGEAPNILQVFDAGAATIMNAKGVAKPVQDilvesgynfnsnDYLA 120
Cdd:COG1840   1 LLEAFEK-KTGIKVNVVRGG--SGELLARLKAEGGNPPADVVWSGDADALEQLANEGLLQPYKS------------PELD 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 84375517 121 GVRNFYADNQGKMVGmpFNSSTPVLYYNKDLLAEvgADAPKTYEEL 166
Cdd:COG1840  66 AIPAEFRDPDGYWFG--FSVRARVIVYNTDLLKE--LGVPKSWEDL 107
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-174 2.50e-03

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 40.03  E-value: 2.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  51 DYKITPIYKGSYTETLTAGIAAyraGEAPNILQVFDAGAATIMNAKGVAKPVQDILvesgynfnsnDYLAGVRNFYAD-- 128
Cdd:cd13583  33 KFKRTPIPSSDYETKRSLLIAS---GDAPDIIPVLYPGEENEFVASGALLPISDYL----------DYMPNYKKYVEKwg 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84375517 129 --------NQ--GKMVGMP-------FNSStpvLYYNKDLLAEVGADAPKTYEELEVVAKKLK 174
Cdd:cd13583 100 lgkelatgRQsdGKYYSLPglhedpgVQYS---FLYRKDIFEKAGIKIPTTWDEFYAALKKLK 159
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-353 7.91e-03

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 38.35  E-value: 7.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517   1 MNKLILAGVLSATAAMPAFATTQVtwwHAMGGQL-----GETVNK-IATDFnasQDDYKITPIYkgSYTETLTAGIAAYR 74
Cdd:COG0687   1 MSRRSLLGLAAAALAAALAGGAPA---AAAEGTLnvynwGGYIDPdVLEPF---EKETGIKVVY--DTYDSNEEMLAKLR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  75 AGEAPnilqvFD-----AGAATIMNAKGVAKPVQDILVEsgynfNSNDYLAGVRNFYADnQGKMVGMPFNSSTPVLYYNK 149
Cdd:COG0687  73 AGGSG-----YDvvvpsDYFVARLIKAGLLQPLDKSKLP-----NLANLDPRFKDPPFD-PGNVYGVPYTWGTTGIAYNT 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 150 DLLAEvgadAPKTYEELevVAKKLKaeGHIAFSQSltpwimfenfkSRHNLPVSDQNNGYDGLSTkimfNTKDMMMHVSK 229
Cdd:COG0687 142 DKVKE----PPTSWADL--WDPEYK--GKVALLDD-----------PREVLGAALLYLGYDPNST----DPADLDAAFEL 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517 230 MKEWSvlGYYKYYGSDWDANQTPFERQEVAMWMGSSGSFGGLRNRVPfelgttylPyWKSVNPDAG-LTFIGGAALFAln 308
Cdd:COG0687 199 LIELK--PNVRAFWSDGAEYIQLLASGEVDLAVGWSGDALALRAEGP--------P-IAYVIPKEGaLLWFDNMAIPK-- 265

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 84375517 309 ghDQQQDKGVAAFFDYLTKPETQVYWHKTTGYVPVTTAAYELAKE 353
Cdd:COG0687 266 --GAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELLPP 308
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
 57-182 7.98e-03

Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts 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 ferric iron-binding 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: 270264 [Multi-domain]  Cd Length: 258  Bit Score: 38.01  E-value: 7.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84375517  57 IYKGSYTETLTAGIAAYRagEAPNI-LQVFDAGAATIMN--AKGVAKPVQDILVESGYN--FNSNDYL--------AGVR 123
Cdd:cd13546   4 VYSPNSEEIIEPIIKEFE--EKPGIkVEVVTGGTGELLAriKAEADNPQADVMWGGGIEtlEAYKDLFepyespeaAAIP 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 84375517 124 NFYADNQGKMVGmpFNSSTPVLYYNKDLLAEvgADAPKTYEELevVAKKLKaeGHIAFS 182
Cdd:cd13546  82 DAYKSPEGLWTG--FSVLPVVLMVNTDLVKN--IGAPKGWKDL--LDPKWK--GKIAFA 132
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH