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Conserved domains on  [gi|507034248|ref|WP_016105945|]
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MULTISPECIES: cell wall hydrolase [Bacillus]

Protein Classification

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, ...
 142-265 1.01e-53

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: 169.97  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248 142 SSISEKEKDLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikhgYAFTPVTDGRINQPASAEAKMA 221
Cdd:COG3773    1 IAYSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 507034248 222 VEEAIstNGIHSD----WLYFYNPKTSTSKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   77 ARDAL--NGWRRDptggALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
22-145 3.92e-15

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 74.73  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  22 NQGATEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNI-PGSMKSNEVTVHQN-------DKPKNI 93
Cdd:PRK06347 323 NTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVsAGSTTSDTNTSKPStgtstskPSTGTS 402

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 507034248  94 SGQIIYQVQPGDSLETIAKRYNVTVQSIKQINNTVGNKLYTGQHVKINSSIS 145
Cdd:PRK06347 403 TNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 454
 
Name Accession Description Interval E-value
CwlJ COG3773
Cell wall hydrolase CwlJ, involved in spore germination [Cell cycle control, cell division, ...
 142-265 1.01e-53

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: 169.97  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248 142 SSISEKEKDLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikhgYAFTPVTDGRINQPASAEAKMA 221
Cdd:COG3773    1 IAYSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 507034248 222 VEEAIstNGIHSD----WLYFYNPKTSTSKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   77 ARDAL--NGWRRDptggALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
spore_SleB TIGR02869
spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme ...
 134-265 4.12e-45

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: 150.60  E-value: 4.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  134 TGQHVKINSS--ISEKEKDLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikhgYAFTPVTDGRIN 211
Cdd:TIGR02869  71 TTQASSANSGngYSQNDIQLLARLVNGEARGEPYEGQVAVAAVILNRVRDPRFPNTIAGVIYQP----GAFTAVADGQIW 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 507034248  212 QPASAEAKMAVEEAIS----TNGIhsdwLYFYNPKTSTSKWITTRQTVAVIGNHVFAK 265
Cdd:TIGR02869 147 LTPTETSKKAALDALNgwdpSGGA----LYYFNPATATSSWIWTRPIIKRIGKHIFCK 200
Hydrolase_2 pfam07486
Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most ...
 162-264 1.25e-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: 135.72  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  162 GESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikhgYAFTPVTDGRINQPASAEAKMAVEEAIS-----TNGihsdWL 236
Cdd:pfam07486   1 GEPYEGQVAVANVILNRVRSPRFPNTICGVVYQP----GQFSPVCDGRINLPPSEEAIRAARDALAgerdpTGG----AL 72

                          90       100
                  ....*....|....*....|....*....
gi 507034248  237 YFYNPKTSTSKWITTRQT-VAVIGNHVFA 264
Cdd:pfam07486  73 YFHNPSVAPSSWIWSRGVrTARIGNHVFY 101
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
22-145 3.92e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 74.73  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  22 NQGATEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNI-PGSMKSNEVTVHQN-------DKPKNI 93
Cdd:PRK06347 323 NTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVsAGSTTSDTNTSKPStgtstskPSTGTS 402

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 507034248  94 SGQIIYQVQPGDSLETIAKRYNVTVQSIKQINNTVGNKLYTGQHVKINSSIS 145
Cdd:PRK06347 403 TNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 454
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
13-76 4.03e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.50  E-value: 4.03e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507034248  13 SAAAITFVCNQGATEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNIPGS 76
Cdd:COG1388   93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 32-74 5.85e-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: 5.85e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 507034248   32 HTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNIP 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 7.61e-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: 55.95  E-value: 7.61e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 507034248  30 TIHTVKKNDTLWGISKQYGVSIQSIKQANN-KGNDQTFIGEQLNI 73
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPlINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
31-73 8.44e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 50.14  E-value: 8.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 507034248    31 IHTVKKNDTLWGISKQYGVSIQSIKQANN-KGNDQTFIGEQLNI 73
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 1.92e-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: 43.63  E-value: 1.92e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 507034248   34 VKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFI--GEQLNIP 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, ...
 142-265 1.01e-53

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: 169.97  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248 142 SSISEKEKDLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikhgYAFTPVTDGRINQPASAEAKMA 221
Cdd:COG3773    1 IAYSDSDLDLLARAIYAEARGEPYEGQVAVAAVVLNRVRSPRFPNTICGVVYQP----GQFSPVCDGQINRPPEEEARRA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 507034248 222 VEEAIstNGIHSD----WLYFYNPKTSTSKWITTRQTVAVIGNHVFAK 265
Cdd:COG3773   77 ARDAL--NGWRRDptggALYFHNPATVTPSWARSRPKTARIGNHVFYR 122
spore_SleB TIGR02869
spore cortex-lytic enzyme; Members of this protein family are the spore cortex-lytic enzyme ...
 134-265 4.12e-45

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: 150.60  E-value: 4.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  134 TGQHVKINSS--ISEKEKDLMARLVTAEAGGESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikhgYAFTPVTDGRIN 211
Cdd:TIGR02869  71 TTQASSANSGngYSQNDIQLLARLVNGEARGEPYEGQVAVAAVILNRVRDPRFPNTIAGVIYQP----GAFTAVADGQIW 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 507034248  212 QPASAEAKMAVEEAIS----TNGIhsdwLYFYNPKTSTSKWITTRQTVAVIGNHVFAK 265
Cdd:TIGR02869 147 LTPTETSKKAALDALNgwdpSGGA----LYYFNPATATSSWIWTRPIIKRIGKHIFCK 200
Hydrolase_2 pfam07486
Cell Wall Hydrolase; These enzymes have been implicated in cell wall hydrolysis, most ...
 162-264 1.25e-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: 135.72  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  162 GESYKGKVAVAKVILNRVNAKGFPNTITGVIYEPikhgYAFTPVTDGRINQPASAEAKMAVEEAIS-----TNGihsdWL 236
Cdd:pfam07486   1 GEPYEGQVAVANVILNRVRSPRFPNTICGVVYQP----GQFSPVCDGRINLPPSEEAIRAARDALAgerdpTGG----AL 72

                          90       100
                  ....*....|....*....|....*....
gi 507034248  237 YFYNPKTSTSKWITTRQT-VAVIGNHVFA 264
Cdd:pfam07486  73 YFHNPSVAPSSWIWSRGVrTARIGNHVFY 101
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
22-145 3.92e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 74.73  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  22 NQGATEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNI-PGSMKSNEVTVHQN-------DKPKNI 93
Cdd:PRK06347 323 NTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVsAGSTTSDTNTSKPStgtstskPSTGTS 402

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 507034248  94 SGQIIYQVQPGDSLETIAKRYNVTVQSIKQINNTVGNKLYTGQHVKINSSIS 145
Cdd:PRK06347 403 TNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 454
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
22-140 6.93e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 73.96  E-value: 6.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  22 NQGATEAST---IHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNIPGSMKSNEVTVHQ--NDKPKNiSGQ 96
Cdd:PRK06347 469 SKPSTNTNTnakVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKpsTNKPSN-STV 547

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 507034248  97 IIYQVQPGDSLETIAKRYNVTVQSIKQINNTVGNKLYTGQHVKI 140
Cdd:PRK06347 548 KTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
13-76 4.03e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.50  E-value: 4.03e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507034248  13 SAAAITFVCNQGATEASTIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNIPGS 76
Cdd:COG1388   93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
22-145 5.98e-13

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 68.18  E-value: 5.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  22 NQGATEAST---IHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNIPGSMKSNEVTVH-------QNDKPK 91
Cdd:PRK06347 395 SKPSTGTSTnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKpstntntSKPSTN 474

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 507034248  92 NISGQIIYQVQPGDSLETIAKRYNVTVQSIKQINNTVGNKLYTGQHVKINSSIS 145
Cdd:PRK06347 475 TNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 528
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 29-135 1.70e-12

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 66.68  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  29 STIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNIPGSMKSNEVTvhqndkpkNISGQIIYQVQPGDSLE 108
Cdd:PRK10783 343 SRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLA--------NNSDSITYRVRKGDSLS 414

                         90       100
                 ....*....|....*....|....*..
gi 507034248 109 TIAKRYNVTVQSIKQINNTVGNKLYTG 135
Cdd:PRK10783 415 SIAKRHGVNIKDVMRWNSDTAKNLQPG 441
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
86-140 1.93e-11

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 60.88  E-value: 1.93e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 507034248  86 QNDKPKNISGQIIYQVQPGDSLETIAKRYNVTVQSIKQINNTVGNKLYTGQHVKI 140
Cdd:COG1388   99 RRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 32-74 5.85e-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: 5.85e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 507034248   32 HTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNIP 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 7.61e-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: 55.95  E-value: 7.61e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 507034248  30 TIHTVKKNDTLWGISKQYGVSIQSIKQANN-KGNDQTFIGEQLNI 73
Cdd:cd00118    1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPlINPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 97-140 2.18e-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: 54.80  E-value: 2.18e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 507034248  97 IIYQVQPGDSLETIAKRYNVTVQSIKQINNTVG-NKLYTGQHVKI 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 4.65e-10

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: 53.55  E-value: 4.65e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 507034248   99 YQVQPGDSLETIAKRYNVTVQSIKQINNTVGNKLYTGQHVKI 140
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
LysM smart00257
Lysin motif;
31-73 8.44e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 50.14  E-value: 8.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 507034248    31 IHTVKKNDTLWGISKQYGVSIQSIKQANN-KGNDQTFIGEQLNI 73
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
98-140 1.46e-08

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 49.75  E-value: 1.46e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 507034248    98 IYQVQPGDSLETIAKRYNVTVQSIKQINNTVG-NKLYTGQHVKI 140
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 69-149 2.79e-08

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 53.97  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248  69 EQLNipGSMKSNEVTVHQNDK--PKNISGQIIYQVQPGDSLETIAKRYNVTVQSIKQINNTVGNKLYTGQHVKINSSISE 146
Cdd:PRK10783 316 DQLR--ESLASGEIAAVQSTLvaDNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSA 393


                 ...
gi 507034248 147 KEK 149
Cdd:PRK10783 394 QRL 396
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 1-74 5.19e-07

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: 48.46  E-value: 5.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248   1 MKLLKIKHIIPLSAAAITFVCN--QGATEASTIHTVKKNDTLWGISKQY---GVSIQSIKQANNKG--N-DQTFIGEQLN 72
Cdd:COG1652   79 MRAGAAAKLSPAVTVAEEAAAPsaELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANRDQikNpDLIYPGQVLR 158


                 ..
gi 507034248  73 IP 74
Cdd:COG1652  159 IP 160
PRK13914 PRK13914
invasion associated endopeptidase;
29-79 1.80e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 48.64  E-value: 1.80e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 507034248  29 STIHTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNIPGSMKS 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 1.92e-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: 43.63  E-value: 1.92e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 507034248   34 VKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFI--GEQLNIP 74
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLSNPNLIypGMKIKIP 43
PRK13914 PRK13914
invasion associated endopeptidase;
4-73 2.97e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 41.71  E-value: 2.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507034248   4 LKIKHIIPLSAAAITFVCNQGATEASTIhTVKKNDTLWGISKQYGVSIQSIKQANNKGNDQTFIGEQLNI 73
Cdd:PRK13914   3 MKKATIAATAGIAVTAFAAPTIASASTV-VVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 24-74 2.69e-03

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 37.20  E-value: 2.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507034248  24 GATEASTIHTVKKNDTLWGISKQY---GVSIQSIKQANN---KGNDQTFIGEQLNIP 74
Cdd:PRK11198  90 TPAPESQFYTVKSGDTLSAIAKKVygnANKYNKIFEANKpmlKSPDKIYPGQVLRIP 146
 
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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