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Conserved domains on  [gi|738755008|ref|WP_036648534|]
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MULTISPECIES: murein transglycosylase D [Enterobacterales]

Protein Classification

murein transglycosylase D( domain architecture ID 11484940)

membrane-bound lytic murein transglycosylase D catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acetyl-D-glucosamine (GlcNAc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-457 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


:

Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 897.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008   1 MKAKAILLASVLLVGCQASRNDANiPVQHAQSLSSAGQGENGKYGDrllSPRWQDDGTSLAEDTDLWNHISDELKMGIPE 80
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSKNDAT-VQQHAQSLSSAGQGEAGKYTS---QARWMDDGTSIAPDQDLWAFIGDELKMGIPE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008  81 NSRIREQKTKFLKNKSYLHDVTLRAEPYMYWIVEQIQKRKMPMELVLLPIVESAFDPHATSSANAAGIWQIVAQTGKNYG 160
Cdd:PRK10783  77 NSRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 161 LKQNQWYDGRRDVVASTKVALDMMQRLNGMFDGDWLLTIAAYNSGEGRVLKAMKQNKARGKPTDFWNLSLPRETTVYVPK 240
Cdd:PRK10783 157 LKQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 241 MLALSEILKNNKRYGIKLPTPNESRALARVEVGQQIELTQAADMAGMSLSKLKTFNAGYKNGATAPNGPHYIMVPKSNVA 320
Cdd:PRK10783 237 MLALSDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHAD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 321 KLRDSLASGDIASVQPTEMAKVSAA-GNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTV-SGKASTQL 398
Cdd:PRK10783 317 QLRESLASGEIAAVQSTLVADNTPLnSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIgAGSSAQRL 396

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 399 ADNGNSITYRVRKGDSFASIAKRHGVNTKDVMRWNSD-AKDIQPGDKLTLFVNNSATPDT 457
Cdd:PRK10783 397 ANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDtAKNLQPGDKLTLFVKNNSTPDS 456
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-457 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 897.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008   1 MKAKAILLASVLLVGCQASRNDANiPVQHAQSLSSAGQGENGKYGDrllSPRWQDDGTSLAEDTDLWNHISDELKMGIPE 80
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSKNDAT-VQQHAQSLSSAGQGEAGKYTS---QARWMDDGTSIAPDQDLWAFIGDELKMGIPE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008  81 NSRIREQKTKFLKNKSYLHDVTLRAEPYMYWIVEQIQKRKMPMELVLLPIVESAFDPHATSSANAAGIWQIVAQTGKNYG 160
Cdd:PRK10783  77 NSRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 161 LKQNQWYDGRRDVVASTKVALDMMQRLNGMFDGDWLLTIAAYNSGEGRVLKAMKQNKARGKPTDFWNLSLPRETTVYVPK 240
Cdd:PRK10783 157 LKQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 241 MLALSEILKNNKRYGIKLPTPNESRALARVEVGQQIELTQAADMAGMSLSKLKTFNAGYKNGATAPNGPHYIMVPKSNVA 320
Cdd:PRK10783 237 MLALSDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHAD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 321 KLRDSLASGDIASVQPTEMAKVSAA-GNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTV-SGKASTQL 398
Cdd:PRK10783 317 QLRESLASGEIAAVQSTLVADNTPLnSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIgAGSSAQRL 396

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 399 ADNGNSITYRVRKGDSFASIAKRHGVNTKDVMRWNSD-AKDIQPGDKLTLFVNNSATPDT 457
Cdd:PRK10783 397 ANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDtAKNLQPGDKLTLFVKNNSTPDS 456
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 116-246 1.71e-60

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: 193.50  E-value: 1.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 116 IQKRKMPMELVLLPIVESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNQWYDGRRDVVASTKVALDMMQRLNGMFdGDW 195
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 738755008 196 LLTIAAYNSGEGRVLKAMKQNKArGKPTDFWNLSLPRETTVYVPKMLALSE 246
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGT-DKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 96-251 2.30e-38

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: 139.36  E-value: 2.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008  96 SYLHDVTLRAEPYMYWIVEQIQKRKMPMELVL-LPIVESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNQ--WYDGRRD 172
Cdd:COG0741   91 ALAALLLRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLgpSPDDLFD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 173 VVASTKVALDMMQRLNGMFDGDWLLTIAAYNSGEGRVLKAMKQNKARgkptdFWNlSLP-RETTVYVPKMLALSEILKNN 251
Cdd:COG0741  171 PETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGE-IIPyAETRNYVKKVLANYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 111-221 9.14e-32

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: 117.41  E-value: 9.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008  111 WIVEQIQKRKMPMELVLLPIVESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNQWYDGRRDVVASTKVALDMMQRLNGM 190
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 738755008  191 FDGDWLLTIAAYNSGEGRVLKAMKQNKARGK 221
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDK 111
LysM smart00257
Lysin motif;
349-390 7.44e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.99  E-value: 7.44e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 738755008   349 YTVRKGDTLSGIASKLGVSVSALKQQNNLRSAS-VRTGQTLTV 390
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-457 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 897.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008   1 MKAKAILLASVLLVGCQASRNDANiPVQHAQSLSSAGQGENGKYGDrllSPRWQDDGTSLAEDTDLWNHISDELKMGIPE 80
Cdd:PRK10783   1 MKAKAILLASVLLVGCQSSKNDAT-VQQHAQSLSSAGQGEAGKYTS---QARWMDDGTSIAPDQDLWAFIGDELKMGIPE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008  81 NSRIREQKTKFLKNKSYLHDVTLRAEPYMYWIVEQIQKRKMPMELVLLPIVESAFDPHATSSANAAGIWQIVAQTGKNYG 160
Cdd:PRK10783  77 NSRIREQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 161 LKQNQWYDGRRDVVASTKVALDMMQRLNGMFDGDWLLTIAAYNSGEGRVLKAMKQNKARGKPTDFWNLSLPRETTVYVPK 240
Cdd:PRK10783 157 LKQTRWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 241 MLALSEILKNNKRYGIKLPTPNESRALARVEVGQQIELTQAADMAGMSLSKLKTFNAGYKNGATAPNGPHYIMVPKSNVA 320
Cdd:PRK10783 237 MLALSDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHAD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 321 KLRDSLASGDIASVQPTEMAKVSAA-GNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTV-SGKASTQL 398
Cdd:PRK10783 317 QLRESLASGEIAAVQSTLVADNTPLnSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIgAGSSAQRL 396

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 399 ADNGNSITYRVRKGDSFASIAKRHGVNTKDVMRWNSD-AKDIQPGDKLTLFVNNSATPDT 457
Cdd:PRK10783 397 ANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDtAKNLQPGDKLTLFVKNNSTPDS 456
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 116-246 1.71e-60

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: 193.50  E-value: 1.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 116 IQKRKMPMELVLLPIVESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNQWYDGRRDVVASTKVALDMMQRLNGMFdGDW 195
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 738755008 196 LLTIAAYNSGEGRVLKAMKQNKArGKPTDFWNLSLPRETTVYVPKMLALSE 246
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGT-DKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 96-251 2.30e-38

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: 139.36  E-value: 2.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008  96 SYLHDVTLRAEPYMYWIVEQIQKRKMPMELVL-LPIVESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNQ--WYDGRRD 172
Cdd:COG0741   91 ALAALLLRRPLPYLPLIEEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLgpSPDDLFD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 173 VVASTKVALDMMQRLNGMFDGDWLLTIAAYNSGEGRVLKAMKQNKARgkptdFWNlSLP-RETTVYVPKMLALSEILKNN 251
Cdd:COG0741  171 PETNIRAGAAYLRELLDRFDGDLVLALAAYNAGPGRVRRWLRRNGDR-----DGE-IIPyAETRNYVKKVLANYAIYRAG 244
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 94-250 4.23e-34

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 132.11  E-value: 4.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008  94 NKSYLHDVTLRAEPYMYWIVEQIQKRKMPME-LVLLPIVESAFDPHATSSANAAGIWQIVAQTGKNYGLkqnqwyDGRRD 172
Cdd:COG4623  250 TRAFLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGARGLMQLMPATAKELGV------DDRLD 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 173 VVASTKVALDMMQRLNGMFD------GDWLLTIAAYNSGEGRVLKAMKQNKARGKPTDFWNLS-------------LPRE 233
Cdd:COG4623  324 PEQSIRAGAKYLRWLYDRFPeaidepDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDRWFDVeksqpkyydtgyaRGRE 403

                        170
                 ....*....|....*..
gi 738755008 234 TTVYVPKMLALSEILKN 250
Cdd:COG4623  404 TVNYVPNIRAYYDIYKR 420
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 111-221 9.14e-32

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: 117.41  E-value: 9.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008  111 WIVEQIQKRKMPMELVLLPIVESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNQWYDGRRDVVASTKVALDMMQRLNGM 190
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 738755008  191 FDGDWLLTIAAYNSGEGRVLKAMKQNKARGK 221
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDK 111
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
255-393 4.76e-16

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 75.52  E-value: 4.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 255 GIKLPTPNESRALARVEVGQQIELTQAADMAGMSLSKLKTFNAGYKNGATAPNGPHYIMVPKSNVAKLRDSLASGDIASV 334
Cdd:COG1388    1 GLLLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738755008 335 QPTEMAKVSAAGN-----------------SYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTVSGK 393
Cdd:COG1388   81 AAAARYTVKSGDTlsgiarrygaaaapspvTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 107-243 1.74e-15

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: 73.28  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 107 PYMYWIVEQIQKRKMPMELVLlPIV--ESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNQWYDGRRDV-VASTKVAL-- 181
Cdd:cd13401    5 PYRDLVERAAKKNGLDPALVY-AIIrqESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDLfDPEYNIRLgs 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738755008 182 ----DMMQRlngmFDGDWLLTIAAYNSGEGRVLKAMKQNkaRGKPTDFWNLSLP-RETTVYVPKMLA 243
Cdd:cd13401   84 aylaELLDR----FDGNPVLALAAYNAGPGRVRRWLKRR--GDLDPDLWIETIPfSETRNYVKRVLE 144
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 131-243 2.10e-15

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: 71.86  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 131 VESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNqwyDGRRDVVASTKVALDMMQRLNGMFDGDWLLTIAAYNSGEGRVL 210
Cdd:cd00254   10 VESGFNPRAVSPAGARGLMQLMPGTARDLGRRGV---DDLFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPGAVD 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 738755008 211 KAmkqnKARGKPtdfwnlsLPRETTVYVPKMLA 243
Cdd:cd00254   87 RW----GGGEVP-------PYKETRNYVQRVLA 108
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
325-447 3.98e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 71.26  E-value: 3.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 325 SLASGDIASVQPTemAKVSAAGNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTVSG----------KA 394
Cdd:PRK06347 460 SKPSTNTNTSKPS--TNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAgsttnntntaKP 537

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738755008 395 STQLADNGNSITYRVRKGDSFASIAKRHGVNTKDVMRWNS-DAKDIQPGDKLTL 447
Cdd:PRK06347 538 STNKPSNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKlTSNMIHVGQKLTI 591
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
343-457 9.36e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 70.11  E-value: 9.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 343 SAAGNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTVSGKASTQL----------------ADNGNSIT 406
Cdd:PRK06347 402 STNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTntskpstntntskpstNTNTNAKV 481

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 738755008 407 YRVRKGDSFASIAKRHGVNTKDVMRWNSDAKD-IQPGDKL------TLFVNNSATPDT 457
Cdd:PRK06347 482 YTVAKGDSLWRIANNNKVTIANLKSWNNLKSDfIYPGQKLkvsagsTTNNTNTAKPST 539
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 349-390 1.46e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 61.64  E-value: 1.46e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 738755008  349 YTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTV 390
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 132-226 1.84e-12

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: 64.86  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 132 ESAFDPHATSSANAAGIWQIVAQTGKNYGLKQnqwydgRRDVVASTKVALDMMQRLNGMFDGD------WLLTIAAYNSG 205
Cdd:cd13403   22 ESRFNPNARSPAGARGLMQLMPSTARELGVND------RLDPEQNIHAGAKYLRYLRDRFPPDidepdrLKFALAAYNAG 95

                         90       100
                 ....*....|....*....|.
gi 738755008 206 EGRVLKAMKQNKARGKPTDFW 226
Cdd:cd13403   96 PGHVRDARRLAKKYGLNPNVW 116
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
328-457 1.91e-12

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 69.34  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 328 SGDIASVQPTEMAKVSAAGNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTVSGKASTQLADNG----- 402
Cdd:PRK06347 312 SGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSkpstg 391

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738755008 403 ------------NSITYRVRKGDSFASIAKRHGVNTKDVMRWNSDAKD-IQPGDKLTLFVNNSATPDT 457
Cdd:PRK06347 392 tstskpstgtstNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDfIYPGQKLKVSAGSTSNTNT 459
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 131-242 1.71e-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: 59.06  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 131 VESAFDPHATSSANAAGIWQIVAQTGKnYGLKQNQWYDGRRDVVASTKVALDM----MQRLNGMFDGDWLLTIAAYNSGE 206
Cdd:cd16896   28 VESNFNPNAVSSKGAIGLMQIMPETAE-WIAEKLGLEDFSEDDLYDPETNIRLgtwyLSYLLKEFDGNLVLALAAYNAGP 106

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 738755008 207 GRVLKAMKQNKARGKPTDFWNLSLPrETTVYVPKML 242
Cdd:cd16896  107 GNVDKWLKDGGWSGDGKTLDQIPFP-ETRHYVKKVL 141
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 348-390 2.33e-10

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 55.57  E-value: 2.33e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 738755008 348 SYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASV-RTGQTLTV 390
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCiYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 405-447 3.04e-10

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 55.18  E-value: 3.04e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 738755008 405 ITYRVRKGDSFASIAKRHGVNTKDVMRWN--SDAKDIQPGDKLTL 447
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANplINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
349-390 7.44e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.99  E-value: 7.44e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 738755008   349 YTVRKGDTLSGIASKLGVSVSALKQQNNLRSAS-VRTGQTLTV 390
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 407-447 1.78e-09

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 53.17  E-value: 1.78e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 738755008  407 YRVRKGDSFASIAKRHGVNTKDVMRWNS-DAKDIQPGDKLTL 447
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGlSSPNLYVGQKLKI 42
LysM smart00257
Lysin motif;
406-447 5.92e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 51.68  E-value: 5.92e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 738755008   406 TYRVRKGDSFASIAKRHGVNTKDVMRWN--SDAKDIQPGDKLTL 447
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNniLDPDNLQVGQKLKI 44
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 111-212 9.84e-09

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: 54.49  E-value: 9.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 111 WIVEQIQKRKMPMELVLLPI-VESAFDPHATSSANAAGIWQIVAQTGknyGLKQNQWYDGRRDVVAS-----------TK 178
Cdd:cd16893    2 IVEKYAKKYGVDPALILAIIeTESSFNPYAVSHSPAYGLMQIVPSTA---GRDVYRLLGGKGGLPSKsylfdpennidIG 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 738755008 179 VA-LDMMQR--LNGMFDGDWL--LTIAAYNSGEGRVLKA 212
Cdd:cd16893   79 TAyLHILQNryLKGIKNPKSReyCAIAAYNGGAGNVLRT 117
PRK13914 PRK13914
invasion associated endopeptidase;
340-450 1.92e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 50.19  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 340 AKVSAAGNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTVSGKASTQLADNGNSITY-RVRKG----DS 414
Cdd:PRK13914  21 APTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAEKTEKSVSATWlNVRSGagvdNS 100

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 738755008 415 FASIAK---RHGVNTKDVMRWNSdakdIQPGDKLTLFVN 450
Cdd:PRK13914 101 IITSIKggtKVTVETTESNGWHK----ITYNDGKTGFVN 135
PHA00368 PHA00368
internal virion protein D
 131-208 1.05e-05

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 48.24  E-value: 1.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738755008  131 VESAFDPHATSSANAAGIWQIVAQTGKNYGLKQNQwyDGRRDVVASTKVALDMMQRLNGMFDGDWLLTIAAYNSGEGR 208
Cdd:PHA00368   35 DESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDD--DDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGR 110
nlpD PRK10871
murein hydrolase activator NlpD;
341-406 2.05e-05

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 46.37  E-value: 2.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738755008 341 KVSAAGNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSA-SVRTGQTLTVsGKASTQLADNGNSIT 406
Cdd:PRK10871  55 KGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPySLNVGQTLQV-GNASGTPITGGNAIT 120
PRK13914 PRK13914
invasion associated endopeptidase;
332-396 4.18e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 45.95  E-value: 4.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738755008 332 ASVQPTEMAKVSAAGNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTVSGKAST 396
Cdd:PRK13914 185 KVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANT 249
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 131-212 4.75e-05

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: 42.30  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 131 VESAFDPHA-TSSANAAGIWQIVAQTGKNYGLKQNQwyDGRRDV------VAStkvALDMMQR----LNGMFDGDWLLTI 199
Cdd:cd13399   14 VESGFGPNAgGSPAGAQGIAQFMPSTWKAYGVDGNG--DGKADPfnpedaIAS---AANYLCRhgwdLNAFLGEDNFLAL 88

                         90
                 ....*....|...
gi 738755008 200 AAYNSGEGRVLKA 212
Cdd:cd13399   89 AAYNAGPGAYANA 101
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 124-181 2.71e-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: 38.93  E-value: 2.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 124 ELVLLPIVESAFDPHA--TSSANAAGIWQIVAQTGKNYGLKQnqwYDGRRDVVASTKVAL 181
Cdd:cd00442    1 VLAAIIGQESGGNKPAnaGSGSGAAGLFQFMPGTWKAYGKNS---SSDLNDPEASIEAAA 57
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 332-416 3.34e-04

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 42.73  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 332 ASVQPTEMAKVSAAGNSYTVRKGDTLSGIASKLGVSVSAL-------KQQNNLRsaSVRTGQTLTVSGKASTQLA----- 399
Cdd:COG3061   55 AAAAPAAPAAPEGEWQEYTVQSGDTLSQIFRRLGLSASDLyallaaeGDAKPLS--RLKPGQELRFQLDADGQLQalrye 132

                         90
                 ....*....|....*...
gi 738755008 400 -DNGNSITYRvRKGDSFA 416
Cdd:COG3061  133 vSRLETLLFT-RQGDGFQ 149
PHA00658 PHA00658
putative lysin
 140-282 6.24e-04

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 42.12  E-value: 6.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 140 TSSANAAGIWQIVAQTGKNYG-LKQNQWYDGRRDVVASTKVALDM--MQRLNGMFDGDWLLTIAAYNSGEGRVLKAMKQN 216
Cdd:PHA00658 325 TSPKGAVGIAQVMPDTAPEAAkLAGLPWDENRYRNDAAYNRALGMayFQKQLRDFGGDLPKAYAAYNAGPGALQSALKDA 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 217 KARGkptdfWNLSLPRETTVYV----------------PKMLALSEILKNNKRygikLPTPNESRALARVEVGQQIELTQ 280
Cdd:PHA00658 405 KDGN-----WLALLPKETQDYVvknmqaynagqgrparPTLADIEAQLQNDPR----LAGNPERLKIARVEAERQFNMQT 475


                 ..
gi 738755008 281 AA 282
Cdd:PHA00658 476 AA 477
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 399-451 8.96e-04

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 41.58  E-value: 8.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738755008 399 ADNGNSITYRVRKGDSFASIAKRHGVNTKDV---MRWNSDAKD---IQPGDKLTLFVNN 451
Cdd:COG3061   64 APEGEWQEYTVQSGDTLSQIFRRLGLSASDLyalLAAEGDAKPlsrLKPGQELRFQLDA 122
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 389-447 2.20e-03

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 38.83  E-value: 2.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738755008 389 TVSGKASTQLADNGnSITYRVRKGDSFASIAKRHgvnTKDVMRWN----------SDAKDIQPGDKLTL 447
Cdd:COG1652   95 EEAAAPSAELAPDA-PKTYTVKPGDTLWGIAKRF---YGDPARWPeiaeanrdqiKNPDLIYPGQVLRI 159
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 297-363 3.56e-03

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 38.06  E-value: 3.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738755008 297 AGYKNGATAPNGPHYIMVPKSNVAKLRDSLASGDIASVQPTEMAKVSAAGNS----------YTVRKGDTLSGIASK 363
Cdd:COG1652   50 AAALPLAAGLAAAVAAAAAAAVLIAPVAVMRAGAAAKLSPAVTVAEEAAAPSaelapdapktYTVKPGDTLWGIAKR 126
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
321-390 3.93e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 39.68  E-value: 3.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738755008 321 KLRDSLASGDIASVQPTEMAKVSAAGNSYTVRKGDTLSGIASKLGVSVSALKQQNNLRSASVRTGQTLTV 390
Cdd:PRK06347 522 KVSAGSTTNNTNTAKPSTNKPSNSTVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
 
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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