NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|550794933|ref|WP_022650424|]
View 

MULTISPECIES: murein transglycosylase D [Enterobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-454 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


:

Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 930.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933   1 MKAKAILLASVLLVGCQ-SQNGSNVQQHAQSLSAAGQGEAGKFTSQARWLDDGTSFAQEQDLWASIGDELKMGIPENSRI 79
Cdd:PRK10783   1 MKAKAILLASVLLVGCQsSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  80 REQKQKYLRNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 159
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 160 RNYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTDFWSLSLPQETKIYVPKMLAL 239
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 240 SDILKNSKRYGVQLPTPDESRALARVRLSSPVDIQQVADMTGMSVSKLKTFNAGVKGSTLGASGPRYVMVPQKHAEQLRE 319
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 320 SLASGEIAAVQSTLIADTSPVSSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNVGAGSSAQRLAKNS 399
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550794933 400 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNNDTD-NLQPGDQLTLFVKNSATPDS 454
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-454 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 930.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933   1 MKAKAILLASVLLVGCQ-SQNGSNVQQHAQSLSAAGQGEAGKFTSQARWLDDGTSFAQEQDLWASIGDELKMGIPENSRI 79
Cdd:PRK10783   1 MKAKAILLASVLLVGCQsSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  80 REQKQKYLRNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 159
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 160 RNYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTDFWSLSLPQETKIYVPKMLAL 239
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 240 SDILKNSKRYGVQLPTPDESRALARVRLSSPVDIQQVADMTGMSVSKLKTFNAGVKGSTLGASGPRYVMVPQKHAEQLRE 319
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 320 SLASGEIAAVQSTLIADTSPVSSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNVGAGSSAQRLAKNS 399
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550794933 400 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNNDTD-NLQPGDQLTLFVKNSATPDS 454
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 111-241 1.19e-61

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: 196.20  E-value: 1.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 111 VKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALDMMQRLNKMFdGDW 190
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550794933 191 LLTVAAYNSGEGRVLKAMKANKArGKSTDFWSLSLPQETKIYVPKMLALSD 241
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGT-DKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 28-246 1.15e-40

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: 145.52  E-value: 1.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  28 AQSLSAAGQGEAGKFTSQARWLDDGTSFAQEQDLWASIGDELKMGIPENSRIREQKQKYLRNKSYLHDVTLRAEPYMYWI 107
Cdd:COG0741   28 AAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 108 AGQVKKRNMPMELVL-LPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQ--TRNYDARRDVVASTTAALDMMQRLNK 184
Cdd:COG0741  108 EEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLglGPSPDDLFDPETNIRAGAAYLRELLD 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550794933 185 MFDGDWLLTVAAYNSGEGRVLKAMKANKARGKStdfwslSLP-QETKIYVPKMLALSDILKNS 246
Cdd:COG0741  188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDRDGE------IIPyAETRNYVKKVLANYAIYRAG 244
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 106-219 1.68e-35

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: 127.42  E-value: 1.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  106 WIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALDMMQRLNKM 185
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 550794933  186 FDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTD 219
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
LysM smart00257
Lysin motif;
403-444 7.83e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.77  E-value: 7.83e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 550794933   403 TYRVRKGDSLSSIAKRHGVNIKDVMRWNN--DTDNLQPGDQLTL 444
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNilDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 1-454 0e+00

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 930.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933   1 MKAKAILLASVLLVGCQ-SQNGSNVQQHAQSLSAAGQGEAGKFTSQARWLDDGTSFAQEQDLWASIGDELKMGIPENSRI 79
Cdd:PRK10783   1 MKAKAILLASVLLVGCQsSKNDATVQQHAQSLSSAGQGEAGKYTSQARWMDDGTSIAPDQDLWAFIGDELKMGIPENSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  80 REQKQKYLRNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 159
Cdd:PRK10783  81 REQKQKYLRNKSYLHDVTLRAEPYMYWIVGQIKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 160 RNYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTDFWSLSLPQETKIYVPKMLAL 239
Cdd:PRK10783 161 RWYDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKANKAKGKPTDFWSLSLPRETKIYVPKMLAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 240 SDILKNSKRYGVQLPTPDESRALARVRLSSPVDIQQVADMTGMSVSKLKTFNAGVKGSTLGASGPRYVMVPQKHAEQLRE 319
Cdd:PRK10783 241 SDILKNSKRYGVRLPTTDESRALARVDLGQQIELAQAAEMAGMSLTKLKTFNAGYKRSTTAPSGPHYIMVPKKHADQLRE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 320 SLASGEIAAVQSTLIADTSPVSSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNVGAGSSAQRLAKNS 399
Cdd:PRK10783 321 SLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNS 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550794933 400 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNNDTD-NLQPGDQLTLFVKNSATPDS 454
Cdd:PRK10783 401 DSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAkNLQPGDKLTLFVKNNSTPDS 456
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 111-241 1.19e-61

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: 196.20  E-value: 1.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 111 VKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALDMMQRLNKMFdGDW 190
Cdd:cd16894    1 LLKEGLPEELKYLALVESGFNPDAVSSAGAAGLWQFMPATAREYGLRVDSWVDERRDPEKSTRAAARYLKDLYKRF-GDW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550794933 191 LLTVAAYNSGEGRVLKAMKANKArGKSTDFWSLSLPQETKIYVPKMLALSD 241
Cdd:cd16894   80 LLALAAYNAGEGRVRRAIKRAGT-DKWEDYYRLYLPAETRRYVPKFLAAKI 129
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 28-246 1.15e-40

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: 145.52  E-value: 1.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  28 AQSLSAAGQGEAGKFTSQARWLDDGTSFAQEQDLWASIGDELKMGIPENSRIREQKQKYLRNKSYLHDVTLRAEPYMYWI 107
Cdd:COG0741   28 AAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLALAALLLRRPLPYLPLI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 108 AGQVKKRNMPMELVL-LPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQ--TRNYDARRDVVASTTAALDMMQRLNK 184
Cdd:COG0741  108 EEAAKKYGVDPALVLaLIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLglGPSPDDLFDPETNIRAGAAYLRELLD 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550794933 185 MFDGDWLLTVAAYNSGEGRVLKAMKANKARGKStdfwslSLP-QETKIYVPKMLALSDILKNS 246
Cdd:COG0741  188 RFDGDLVLALAAYNAGPGRVRRWLRRNGDRDGE------IIPyAETRNYVKKVLANYAIYRAG 244
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 73-245 1.88e-36

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 138.66  E-value: 1.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  73 IPENSRIREQKQKYLRN-----KSYLHDVTLRAEPYMYWIAGQVKKRNMPME-LVLLPIVESAFDPHATSGANAAGIWQI 146
Cdd:COG4623  229 IKKGGTLARLYERYFGHvkrdtRAFLRRIEGRLPPYDPLFEKYAEEYGLDWRlLAALAYQESHWNPRARSPTGARGLMQL 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 147 IPSTGRNYGLKQtrnydaRRDVVASTTAALDMMQRLNKMFD------GDWLLTVAAYNSGEGRVLKAMKANKARGKSTDF 220
Cdd:COG4623  309 MPATAKELGVDD------RLDPEQSIRAGAKYLRWLYDRFPeaidepDRWWFALAAYNAGPGHVQDARRLAKKQGLDPDR 382

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 550794933 221 WSLS-------------LPQETKIYVPKMLALSDILKN 245
Cdd:COG4623  383 WFDVeksqpkyydtgyaRGRETVNYVPNIRAYYDIYKR 420
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 106-219 1.68e-35

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: 127.42  E-value: 1.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  106 WIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALDMMQRLNKM 185
Cdd:pfam01464   1 IIKAAQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVDDLFDPEKNIKAGTKYLKELYKQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 550794933  186 FDGDWLLTVAAYNSGEGRVLKAMKANKARGKSTD 219
Cdd:pfam01464  81 YGGDLWLALAAYNAGPGRVRKWIKNAGAKDKKLL 114
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 126-238 3.05e-19

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: 82.65  E-value: 3.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 126 VESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNydaRRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVL 205
Cdd:cd00254   10 VESGFNPRAVSPAGARGLMQLMPGTARDLGRRGVDD---LFDPEENIRAGARYLRELLDRFGGDLELALAAYNAGPGAVD 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 550794933 206 KAMKANKargkstdfwslSLPQETKIYVPKMLA 238
Cdd:cd00254   87 RWGGGEV-----------PPYKETRNYVQRVLA 108
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 102-238 9.75e-17

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: 77.13  E-value: 9.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 102 PYMYWIAGQVKKRNMPMELVLlPIV--ESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDV-VASTTAALDM 178
Cdd:cd13401    5 PYRDLVERAAKKNGLDPALVY-AIIrqESAFDPDAVSPAGALGLMQLMPATAKDVAKKLGLPYYSPRDLfDPEYNIRLGS 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550794933 179 --MQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKANkaRGKSTDFWSLSLP-QETKIYVPKMLA 238
Cdd:cd13401   84 ayLAELLDRFDGNPVLALAAYNAGPGRVRRWLKRR--GDLDPDLWIETIPfSETRNYVKRVLE 144
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
292-444 1.91e-16

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 76.29  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 292 AGVKGSTLGASGPRYVMVPQKHAEQLRESLASGEIAAVQSTLIADTSPVSSRSYKVRSGDTLSGIASRLGVnakdlqqwn 371
Cdd:COG1388   33 VALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGA--------- 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550794933 372 nlrgsglkvgqtlnvgagssaqrlAKNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNN-DTDNLQPGDQLTL 444
Cdd:COG1388  104 ------------------------AAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGlSSDTIRPGQKLKI 153
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 127-222 2.59e-15

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: 73.34  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 127 ESAFDPHATSGANAAGIWQIIPSTGRNYGLKQtrnydaRRDVVASTTAALDMMQRLNKMFDGD------WLLTVAAYNSG 200
Cdd:cd13403   22 ESRFNPNARSPAGARGLMQLMPSTARELGVND------RLDPEQNIHAGAKYLRYLRDRFPPDidepdrLKFALAAYNAG 95

                         90       100
                 ....*....|....*....|..
gi 550794933 201 EGRVLKAMKANKARGKSTDFWS 222
Cdd:cd13403   96 PGHVRDARRLAKKYGLNPNVWF 117
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
230-386 4.92e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.43  E-value: 4.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 230 KIYVPKMLALSDILKNSKRYGVQLPTPDESRALARVRLSSPVDIQQVADMTGMSVSKLKTFNAGVKGSTLGASGPRYVMV 309
Cdd:COG1388    3 LLALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550794933 310 PQKHAEQLRESLasGEIAAVQSTliadTSPVSSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNV 386
Cdd:COG1388   83 AARYTVKSGDTL--SGIARRYGA----AAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 126-248 5.92e-14

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: 69.08  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 126 VESAFDPHATSGANAAGIWQIIPSTGR----NYGLKQTRN---YDARRDVVASTTaaldMMQRLNKMFDGDWLLTVAAYN 198
Cdd:cd16896   28 VESNFNPNAVSSKGAIGLMQIMPETAEwiaeKLGLEDFSEddlYDPETNIRLGTW----YLSYLLKEFDGNLVLALAAYN 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 550794933 199 SGEGRVLKAMKANKARGKSTDFWSLSLPqETKIYVPKmlalsdILKNSKR 248
Cdd:cd16896  104 AGPGNVDKWLKDGGWSGDGKTLDQIPFP-ETRHYVKK------VLKNYKI 146
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
337-442 9.75e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 73.19  E-value: 9.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 337 TSPVSSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNVGAGSSAQ---------------RLAKNSDS 401
Cdd:PRK06347 400 GTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNtntskpstntntskpSTNTNTNA 479

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 550794933 402 ITYRVRKGDSLSSIAKRHGVNIKDVMRWNN-DTDNLQPGDQL 442
Cdd:PRK06347 480 KVYTVAKGDSLWRIANNNKVTIANLKSWNNlKSDFIYPGQKL 521
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 345-386 1.00e-13

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: 65.11  E-value: 1.00e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 550794933  345 YKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNV 386
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
341-442 1.73e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 72.42  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 341 SSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNVGAGSSAQ----------------RLAKNSDSITY 404
Cdd:PRK06347 329 NAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSdtntskpstgtstskpSTGTSTNAKVY 408

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 550794933 405 RVRKGDSLSSIAKRHGVNIKDVMRWNN-DTDNLQPGDQL 442
Cdd:PRK06347 409 TVVKGDSLWRIANNNKVTIANLKSWNNlKSDFIYPGQKL 447
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
341-444 2.28e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 72.03  E-value: 2.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 341 SSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNVGAGSSAQRLA---------KNSDSITYRVRKGDS 411
Cdd:PRK06347 478 NAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNtakpstnkpSNSTVKTYTVKKGDS 557

                         90       100       110
                 ....*....|....*....|....*....|....
gi 550794933 412 LSSIAKRHGVNIKDVMRWNNDTDN-LQPGDQLTL 444
Cdd:PRK06347 558 LWAISRQYKTTVDNIKAWNKLTSNmIHVGQKLTI 591
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 404-444 1.12e-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: 62.03  E-value: 1.12e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 550794933  404 YRVRKGDSLSSIAKRHGVNIKDVMRWNN-DTDNLQPGDQLTL 444
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGlSSPNLYVGQKLKI 42
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 402-444 1.58e-12

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: 61.73  E-value: 1.58e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 550794933 402 ITYRVRKGDSLSSIAKRHGVNIKDVMRWNN--DTDNLQPGDQLTL 444
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPliNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
403-444 7.83e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.77  E-value: 7.83e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 550794933   403 TYRVRKGDSLSSIAKRHGVNIKDVMRWNN--DTDNLQPGDQLTL 444
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNilDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 343-386 1.61e-11

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: 58.65  E-value: 1.61e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 550794933 343 RSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSG-LKVGQTLNV 386
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
LysM smart00257
Lysin motif;
345-386 6.22e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 57.07  E-value: 6.22e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 550794933   345 YKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSG-LKVGQTLNV 386
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 112-239 3.54e-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: 55.64  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 112 KKRNMPMELVLLPI-VESAFDPHATSGANAAGIWQIIPSTG------RNYGLKQ--TRNY--DARRDVVAStTAALDMMQ 180
Cdd:cd16893    8 KKYGVDPALILAIIeTESSFNPYAVSHSPAYGLMQIVPSTAgrdvyrLLGGKGGlpSKSYlfDPENNIDIG-TAYLHILQ 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550794933 181 R---------LNKMFdgdwlLTVAAYNSGEGRVLKAMKANKARG------KSTD--FWSLS--LP-QETKIYVPKMLAL 239
Cdd:cd16893   87 NrylkgiknpKSREY-----CAIAAYNGGAGNVLRTFSSDRKKAiskinrLSPDevYQHLTkkLPaAETRNYLKKVLKA 160
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 119-176 6.33e-08

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: 48.95  E-value: 6.33e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 119 ELVLLPIVESAFDPHA--TSGANAAGIWQIIPSTGRNYGLKQTRNydaRRDVVASTTAAL 176
Cdd:cd00442    1 VLAAIIGQESGGNKPAnaGSGSGAAGLFQFMPGTWKAYGKNSSSD---LNDPEASIEAAA 57
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 126-207 4.89e-07

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: 48.07  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 126 VESAFDPHA-TSGANAAGIWQIIPSTGRNYGLkqTRNYDARRDVV----ASTTAALDMMQR---LNKMFDGDWLLTVAAY 197
Cdd:cd13399   14 VESGFGPNAgGSPAGAQGIAQFMPSTWKAYGV--DGNGDGKADPFnpedAIASAANYLCRHgwdLNAFLGEDNFLALAAY 91

                         90
                 ....*....|
gi 550794933 198 NSGEGRVLKA 207
Cdd:cd13399   92 NAGPGAYANA 101
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
352-442 1.46e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 50.46  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 352 TLSGIASRLG--VNAKDLQQWNNLRGSGlkvGQTLNVGAGSSAQRLAKNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRW 429
Cdd:PRK06347 282 TDTAYATKLNdlISRYNLTQYDSGKTTG---GNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAW 358

                         90
                 ....*....|....
gi 550794933 430 NN-DTDNLQPGDQL 442
Cdd:PRK06347 359 NNlKSDFIYPGQKL 372
PHA00368 PHA00368
internal virion protein D
 126-237 1.51e-05

internal virion protein D


Pssm-ID: 222785 [Multi-domain]  Cd Length: 1315  Bit Score: 47.47  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  126 VESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRnyDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVL 205
Cdd:PHA00368   35 DESRFNPTAKSPTGPKGLMQFTKATAKALGLIVDD--DDRLDPELAIDAGARYLADLVGKYDGDELKAALAYNQGEGRLG 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 550794933  206 KAMKANKARGkstDFWSLSlpQETKIYVPKML 237
Cdd:PHA00368  113 APQLEAYDKG---DFASIS--EEGRNYLRNLL 139
PRK13914 PRK13914
invasion associated endopeptidase;
337-386 1.54e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 47.10  E-value: 1.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 550794933 337 TSPV---SSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSGLKVGQTLNV 386
Cdd:PRK13914 191 ETPVvdqNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAI 243
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 403-444 1.57e-05

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: 46.97  E-value: 1.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 550794933 403 TYRVRKGDSLSSIAKRHGVNIKDVMR------WNNDTDNLQPGDQLTL 444
Cdd:COG3061   71 EYTVQSGDTLSQIFRRLGLSASDLYAllaaegDAKPLSRLKPGQELRF 118
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 403-444 3.28e-05

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: 44.23  E-value: 3.28e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 550794933 403 TYRVRKGDSLSSIAKRH---GVNIKDVMRWN----NDTDNLQPGDQLTL 444
Cdd:COG1652  111 TYTVKPGDTLWGIAKRFygdPARWPEIAEANrdqiKNPDLIYPGQVLRI 159
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
99-214 3.72e-05

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 45.81  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933  99 RAEPYMYWIAGQVKKRNMPMELVLLPI-VESAFDPHATSGANAAGIWQIIPST---------------GRNYGLKQTRNY 162
Cdd:PRK11671 188 RAHKYLPMVRKASRKYGVDESLILAIMqTESSFNPYAVSRSDALGLMQVVQHTagkdvfrmkgksgqpSRSYLFDPANNI 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 550794933 163 DArrdvvasTTAALDMMQrlNKMFDGDWLLT------VAAYNSGEGRVLKAMKANKAR 214
Cdd:PRK11671 268 DT-------GTAYLAILQ--NVYLGGITNPTsrryavITAYNGGAGSVLRVFSNDKIQ 316
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 327-384 1.03e-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: 44.27  E-value: 1.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550794933 327 AAVQSTLIADTSPvSSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGSG-----LKVGQTL 384
Cdd:COG3061   55 AAAAPAAPAAPEG-EWQEYTVQSGDTLSQIFRRLGLSASDLYALLAAEGDAkplsrLKPGQEL 116
PHA00658 PHA00658
putative lysin
 135-277 2.99e-04

putative lysin


Pssm-ID: 106967 [Multi-domain]  Cd Length: 720  Bit Score: 43.27  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 135 TSGANAAGIWQIIPSTG----RNYGLKQTRNyDARRDVVASTTAALDMMQRLNKMFDGDWLLTVAAYNSGEGRVLKAMKA 210
Cdd:PHA00658 325 TSPKGAVGIAQVMPDTApeaaKLAGLPWDEN-RYRNDAAYNRALGMAYFQKQLRDFGGDLPKAYAAYNAGPGALQSALKD 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794933 211 NKARGkstdfWSLSLPQETKIYV-------------PKMLALSDI---LKNSKRygvqLPTPDESRALARVRLSSPVDIQ 274
Cdd:PHA00658 404 AKDGN-----WLALLPKETQDYVvknmqaynagqgrPARPTLADIeaqLQNDPR----LAGNPERLKIARVEAERQFNMQ 474


                 ...
gi 550794933 275 QVA 277
Cdd:PHA00658 475 TAA 477
nlpD PRK10871
murein hydrolase activator NlpD;
341-390 7.94e-04

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 41.36  E-value: 7.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550794933 341 SSRSYKVRSGDTLSGIASRLGVNAKDLQQWNNLRGS-GLKVGQTLNVGAGS 390
Cdd:PRK10871  59 SGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPySLNVGQTLQVGNAS 109
 
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