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Conserved domains on  [gi|507052287|ref|WP_016123271|]
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MULTISPECIES: cell wall hydrolase [Bacillus]

Protein Classification

cell wall hydrolase( domain architecture ID 11467324)

cell wall hydrolase similar to Bacillus proteins SleB and CwlJ, which are spore cortex-lytic enzymes involved in the depolymerization of cortex peptidoglycan during germination

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CwlJ COG3773
Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, ...
 144-265 1.97e-52

Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442987  Cd Length: 124  Bit Score: 166.51  E-value: 1.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287 144 ISQKEKNLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikygYAFTPVTDGRINQPASAEAKMAVE 223
Cdd:COG3773    3 YSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRAAR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 507052287 224 EAIstNGVHSD----WLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   79 DAL--NGWRRDptggALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
22-140 9.55e-18

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 82.44  E-value: 9.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  22 SQSTAEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIP-GSVKSNEITV-PQNAKPANiSGQIIY 99
Cdd:PRK06347 472 STNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSaGSTTNNTNTAkPSTNKPSN-STVKTY 550

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 507052287 100 QVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKI 140
Cdd:PRK06347 551 TVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
 
Name Accession Description Interval E-value
CwlJ COG3773
Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, ...
 144-265 1.97e-52

Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442987  Cd Length: 124  Bit Score: 166.51  E-value: 1.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287 144 ISQKEKNLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikygYAFTPVTDGRINQPASAEAKMAVE 223
Cdd:COG3773    3 YSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRAAR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 507052287 224 EAIstNGVHSD----WLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   79 DAL--NGWRRDptggALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
spore_SleB TIGR02869
spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme ...
 144-265 9.28e-44

spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme SleB from Bacillus subtilis and other Gram-positive, endospore-forming bacterial species. This protein is stored in an inactive form in the spore and activated during germination. [Cellular processes, Sporulation and germination]


Pssm-ID: 213747 [Multi-domain]  Cd Length: 200  Bit Score: 147.14  E-value: 9.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  144 ISQKEKNLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikygYAFTPVTDGRINQPASAEAKMAVE 223
Cdd:TIGR02869  83 YSQNDIQLLARLVNGEARGEPYEGQVAVAAVILNRVRDPRFPNTIAGVIYQP----GAFTAVADGQIWLTPTETSKKAAL 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 507052287  224 EAIS----TNGVhsdwLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:TIGR02869 159 DALNgwdpSGGA----LYYFNPATATSSWIWTRPIIKRIGKHIFCK 200
Hydrolase_2 pfam07486
Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most ...
 162-264 1.54e-40

Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most extensively in Bacillus subtilis. For instance Swiss:P50739 is expressed during sporulation as an inactive form and then deposited on the cell outer cortex. During germination the the enzyme is activated and hydrolyses the cortex. A similar role is carried out by the partially redundant Swiss:P42249. It is not clear whether these enzymes are amidases or peptidases.


Pssm-ID: 462179  Cd Length: 101  Bit Score: 135.34  E-value: 1.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  162 GESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikygYAFTPVTDGRINQPASAEAKMAVEEAIS-----TNGVhsdwL 236
Cdd:pfam07486   1 GEPYEGQVAVANVILNRVRSPRFPNTICGVVYQP----GQFSPVCDGRINLPPSEEAIRAARDALAgerdpTGGA----L 72

                          90       100
                  ....*....|....*....|....*....
gi 507052287  237 YFYNPKTSTDKWITTRQT-VAVIGNHVFA 264
Cdd:pfam07486  73 YFHNPSVAPSSWIWSRGVrTARIGNHVFY 101
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
22-140 9.55e-18

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 82.44  E-value: 9.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  22 SQSTAEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIP-GSVKSNEITV-PQNAKPANiSGQIIY 99
Cdd:PRK06347 472 STNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSaGSTTNNTNTAkPSTNKPSN-STVKTY 550

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 507052287 100 QVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKI 140
Cdd:PRK06347 551 TVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
13-76 6.42e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 64.73  E-value: 6.42e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507052287  13 SAAAITFVCSQSTAEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIPGS 76
Cdd:COG1388   93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 97-140 2.10e-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: 57.50  E-value: 2.10e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 507052287  97 IIYQVQPGDSLETIARRYNVTVQSIKQMNNTVG-NKLYTGQHLKI 140
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 99-140 5.45e-11

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: 56.25  E-value: 5.45e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 507052287   99 YQVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKI 140
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
LysM smart00257
Lysin motif;
98-140 9.09e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.83  E-value: 9.09e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 507052287    98 IYQVQPGDSLETIARRYNVTVQSIKQMNNTVG-NKLYTGQHLKI 140
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 34-74 6.41e-06

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 42.48  E-value: 6.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 507052287   34 VKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFI--GEQLHIP 74
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLSNPNLIypGMKIKIP 43
 
Name Accession Description Interval E-value
CwlJ COG3773
Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, ...
 144-265 1.97e-52

Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442987  Cd Length: 124  Bit Score: 166.51  E-value: 1.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287 144 ISQKEKNLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikygYAFTPVTDGRINQPASAEAKMAVE 223
Cdd:COG3773    3 YSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRAAR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 507052287 224 EAIstNGVHSD----WLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   79 DAL--NGWRRDptggALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
spore_SleB TIGR02869
spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme ...
 144-265 9.28e-44

spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme SleB from Bacillus subtilis and other Gram-positive, endospore-forming bacterial species. This protein is stored in an inactive form in the spore and activated during germination. [Cellular processes, Sporulation and germination]


Pssm-ID: 213747 [Multi-domain]  Cd Length: 200  Bit Score: 147.14  E-value: 9.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  144 ISQKEKNLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikygYAFTPVTDGRINQPASAEAKMAVE 223
Cdd:TIGR02869  83 YSQNDIQLLARLVNGEARGEPYEGQVAVAAVILNRVRDPRFPNTIAGVIYQP----GAFTAVADGQIWLTPTETSKKAAL 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 507052287  224 EAIS----TNGVhsdwLYFYNPKTSTDKWITTRQTVAVIGNHVFAK 265
Cdd:TIGR02869 159 DALNgwdpSGGA----LYYFNPATATSSWIWTRPIIKRIGKHIFCK 200
Hydrolase_2 pfam07486
Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most ...
 162-264 1.54e-40

Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most extensively in Bacillus subtilis. For instance Swiss:P50739 is expressed during sporulation as an inactive form and then deposited on the cell outer cortex. During germination the the enzyme is activated and hydrolyses the cortex. A similar role is carried out by the partially redundant Swiss:P42249. It is not clear whether these enzymes are amidases or peptidases.


Pssm-ID: 462179  Cd Length: 101  Bit Score: 135.34  E-value: 1.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  162 GESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikygYAFTPVTDGRINQPASAEAKMAVEEAIS-----TNGVhsdwL 236
Cdd:pfam07486   1 GEPYEGQVAVANVILNRVRSPRFPNTICGVVYQP----GQFSPVCDGRINLPPSEEAIRAARDALAgerdpTGGA----L 72

                          90       100
                  ....*....|....*....|....*....
gi 507052287  237 YFYNPKTSTDKWITTRQT-VAVIGNHVFA 264
Cdd:pfam07486  73 YFHNPSVAPSSWIWSRGVrTARIGNHVFY 101
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
22-140 9.55e-18

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 82.44  E-value: 9.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  22 SQSTAEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIP-GSVKSNEITV-PQNAKPANiSGQIIY 99
Cdd:PRK06347 472 STNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSaGSTTNNTNTAkPSTNKPSN-STVKTY 550

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 507052287 100 QVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKI 140
Cdd:PRK06347 551 TVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
22-150 2.36e-14

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 72.42  E-value: 2.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  22 SQSTAEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIPGSVKSNEITV-----PQNAKPANI--S 94
Cdd:PRK06347 398 STGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSkpstnTNTSKPSTNtnT 477

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 507052287  95 GQIIYQVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKINSTISQKEKN 150
Cdd:PRK06347 478 NAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTN 533
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
24-142 1.06e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 70.49  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  24 STAEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHI-PGSVKSNEITVPQNA-------KPANISG 95
Cdd:PRK06347 325 GNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVsAGSTTSDTNTSKPSTgtstskpSTGTSTN 404

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 507052287  96 QIIYQVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKINS 142
Cdd:PRK06347 405 AKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSA 451
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 14-138 1.17e-13

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 70.15  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  14 AAAITFVCSQSTAEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIPGSVKSNEItvpqnakpANI 93
Cdd:PRK10783 328 AAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRL--------ANN 399

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 507052287  94 SGQIIYQVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHL 138
Cdd:PRK10783 400 SDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
13-76 6.42e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 64.73  E-value: 6.42e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507052287  13 SAAAITFVCSQSTAEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIPGS 76
Cdd:COG1388   93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
83-140 1.77e-12

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 63.57  E-value: 1.77e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 507052287  83 TVPQNAKPANISGQIIYQVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKI 140
Cdd:COG1388   96 GIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 97-140 2.10e-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: 57.50  E-value: 2.10e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 507052287  97 IIYQVQPGDSLETIARRYNVTVQSIKQMNNTVG-NKLYTGQHLKI 140
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 99-140 5.45e-11

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: 56.25  E-value: 5.45e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 507052287   99 YQVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKI 140
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 32-74 8.95e-11

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: 55.87  E-value: 8.95e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 507052287   32 HTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIP 74
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 30-73 1.59e-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: 1.59e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 507052287  30 TIHTVKKNDTLWGISKQYGVSIQSIKQANN-KGNDQTFIGEQLHI 73
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPlINPDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 76-150 8.58e-10

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 58.59  E-value: 8.58e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507052287  76 SVKSNEITVPQNAKPA--NISGQIIYQVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKINSTISQKEKN 150
Cdd:PRK10783 321 SLASGEIAAVQSTLVAdnTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLA 397
LysM smart00257
Lysin motif;
98-140 9.09e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 52.83  E-value: 9.09e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 507052287    98 IYQVQPGDSLETIARRYNVTVQSIKQMNNTVG-NKLYTGQHLKI 140
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
31-71 3.26e-08

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 48.60  E-value: 3.26e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 507052287    31 IHTVKKNDTLWGISKQYGVSIQSIKQANN-KGNDQTFIGEQL 71
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKL 42
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 1-74 1.02e-06

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: 47.69  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287   1 MKLLKLKHIIPLSAAAITFVC--SQSTAEASTIHTVKKNDTLWGISKQY---GVSIQSIKQANNKG--N-DQTFIGEQLH 72
Cdd:COG1652   79 MRAGAAAKLSPAVTVAEEAAApsAELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANRDQikNpDLIYPGQVLR 158


                 ..
gi 507052287  73 IP 74
Cdd:COG1652  159 IP 160
PRK13914 PRK13914
invasion associated endopeptidase;
29-79 1.56e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 48.64  E-value: 1.56e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 507052287  29 STIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHIPGSVKS 79
Cdd:PRK13914 199 ATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANT 249
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 34-74 6.41e-06

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 42.48  E-value: 6.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 507052287   34 VKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFI--GEQLHIP 74
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLSNPNLIypGMKIKIP 43
PRK13914 PRK13914
invasion associated endopeptidase;
4-73 9.70e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 46.33  E-value: 9.70e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287   4 LKLKHIIPLSAAAITFVCSQSTAEASTIhTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLHI 73
Cdd:PRK13914   3 MKKATIAATAGIAVTAFAAPTIASASTV-VVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
87-150 1.85e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 45.46  E-value: 1.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507052287  87 NAKPANISGQIIYQVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKINSTISQKEKN 150
Cdd:PRK06347 321 SSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTN 384
MltG_like cd08010
proteins similar to Escherichia coli YceG/mltG may function as endolytic murein ...
 53-185 9.21e-04

proteins similar to Escherichia coli YceG/mltG may function as endolytic murein transglycosylases; The gene product of Escherichia coli yceG/mltG has been erroneously annotated as an aminodeoxychorismate lyase. Its overexpression has been reported to cause abnormal biofilm architecture, and it has been reported to be part of a putative five-gene operon. More recently it has been proposed to function as a terminase for peptidoglycan polymerization. The family also includes Streptomyces caeruleus NovB, an uncharacterized member of the novobiocin biosynthetic gene cluster.


Pssm-ID: 381750  Cd Length: 246  Bit Score: 39.52  E-value: 9.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  53 SIKQANNKGNDQTFIgEQLHIPGSVKSNEITvpqnakPANISGQII---YQVQPGDSLETIARrynvtvQSIKQMNNTVg 129
Cdd:cd08010   44 KALAKAGGLSEADFL-KALRDPAFLKELGNP------KYPLEGYLFpdtYEVPKGDSAEDILK------RMVKRFNEKL- 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507052287 130 NKLYTGQHLKINSTISQKeknL-MARLVTAEAGGESYKGKvaVAKVILNRVNaKGFP 185
Cdd:cd08010  110 EEAWLERAKLPGLTPYEV---LtLASIVEKEAGLDEERPK--VAGVFYNRLK-KGMP 160
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 74-140 2.33e-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: 37.68  E-value: 2.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507052287  74 PGSVKSNEITVPQNAKPANISGQiiYQVQPGDSLETIARRY---NVTVQSIKQMNNTV---GNKLYTGQHLKI 140
Cdd:COG1652   89 PAVTVAEEAAAPSAELAPDAPKT--YTVKPGDTLWGIAKRFygdPARWPEIAEANRDQiknPDLIYPGQVLRI 159
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 26-74 3.25e-03

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 37.20  E-value: 3.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 507052287  26 AEASTIHTVKKNDTLWGISKQY---GVSIQSIKQANN---KGNDQTFIGEQLHIP 74
Cdd:PRK11198  92 APESQFYTVKSGDTLSAIAKKVygnANKYNKIFEANKpmlKSPDKIYPGQVLRIP 146
PRK13914 PRK13914
invasion associated endopeptidase;
82-161 3.94e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 38.24  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507052287  82 ITVPQNAKPANISGQIIYqVQPGDSLETIARRYNVTVQSIKQMNNTVGNKLYTGQHLKIN--STISQKEKNLMARLVTAE 159
Cdd:PRK13914  14 IAVTAFAAPTIASASTVV-VEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNevAAAEKTEKSVSATWLNVR 92


                 ..
gi 507052287 160 AG 161
Cdd:PRK13914  93 SG 94
 
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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