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Conserved domains on  [gi|1752980735|gb|QEX38173|]
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LysM peptidoglycan-binding domain-containing protein [Staphylococcus lugdunensis]

Protein Classification

LysM and COG3942 domain-containing protein( domain architecture ID 13291756)

LysM and COG3942 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
208-323 1.17e-39

Surface antigen [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 135.89  E-value: 1.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 208 YRTPIFSHSNLYTWGQCTWHVFNRRAAIGKGISTYWWNANNWDNAAAADGYTINYTPTVGSIAQTDI---GYYGHVAFVE 284
Cdd:COG3942    10 YPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTPgvaGPYGHVAVVE 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1752980735 285 RVNSDGSILVSEMNYSAsPGIMTYRTIPSYQVSSYRYIH 323
Cdd:COG3942    90 SVNSDGSILVSEMNWGG-PGIYSTRTISAGNASSYGFIH 127
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
26-196 2.05e-33

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 129.43  E-value: 2.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  26 ATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKVS---------------GSSKSTANRTANTSSSTYT 90
Cdd:PRK06347  330 AKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSagsttsdtntskpstGTSTSKPSTGTSTNAKVYT 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  91 VQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTG--TAAKNNTKPSQSSKSS-----------IYTVQPGDS 157
Cdd:PRK06347  410 VVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAgsTSNTNTSKPSTNTNTSkpstntntnakVYTVAKGDS 489

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1752980735 158 LSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGTAS 196
Cdd:PRK06347  490 LWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 528
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
208-323 1.17e-39

Surface antigen [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 135.89  E-value: 1.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 208 YRTPIFSHSNLYTWGQCTWHVFNRRAAIGKGISTYWWNANNWDNAAAADGYTINYTPTVGSIAQTDI---GYYGHVAFVE 284
Cdd:COG3942    10 YPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTPgvaGPYGHVAVVE 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1752980735 285 RVNSDGSILVSEMNYSAsPGIMTYRTIPSYQVSSYRYIH 323
Cdd:COG3942    90 SVNSDGSILVSEMNWGG-PGIYSTRTISAGNASSYGFIH 127
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
26-196 2.05e-33

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 129.43  E-value: 2.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  26 ATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKVS---------------GSSKSTANRTANTSSSTYT 90
Cdd:PRK06347  330 AKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSagsttsdtntskpstGTSTSKPSTGTSTNAKVYT 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  91 VQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTG--TAAKNNTKPSQSSKSS-----------IYTVQPGDS 157
Cdd:PRK06347  410 VVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAgsTSNTNTSKPSTNTNTSkpstntntnakVYTVAKGDS 489

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1752980735 158 LSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGTAS 196
Cdd:PRK06347  490 LWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 528
PRK08581 PRK08581
amidase domain-containing protein;
219-322 4.51e-18

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 84.84  E-value: 4.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 219 YTWGQCTWHVFNRRAAIGKGISTYWWNANNWDNAAAADGYTINYTPTVGSIAQTDIG------YYGHVAFVERVNSDGSI 292
Cdd:PRK08581  508 YPHGQCTWYVYNRMKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVVFEAGqagadqHYGHVAFVEKVNSDGSI 587

                          90       100       110
                  ....*....|....*....|....*....|
gi 1752980735 293 LVSEMNYSASpGIMTYRTIPSYQVSSYRYI 322
Cdd:PRK08581  588 VISESNVKGL-GIISYRTIDAAAAEELSYI 616
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
42-194 8.77e-17

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 76.29  E-value: 8.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  42 HKYGMSIARLKSLNGLKSNLIFPNQVLKVSGSSKSTANRTANTSSSTYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFF 121
Cdd:COG1388     5 ALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAA 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752980735 122 IYPGQKlKVTGTAAKNNTKPSQSSKSSIYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGT 194
Cdd:COG1388    85 RYTVKS-GDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 89-131 7.74e-15

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: 67.42  E-value: 7.74e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1752980735  89 YTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVT 131
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 217-298 4.66e-14

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 66.68  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 217 NLYTWGQCTWHVFNRRAAIGKgistYWWNANNWDNAAAADGYTINYTPTVGSIAQTDIG----YYGHVAFVERVNsDGSI 292
Cdd:pfam05257   3 NGYPWGQCTWFVYWRVAQLGI----YLGNAGDWADAAAGAYKVGSTTPKVGDIVVFDPGgggaSYGHVAIVEKVN-DGSI 77


                  ....*.
gi 1752980735 293 LVSEMN 298
Cdd:pfam05257  78 TVSEQN 83
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 88-130 2.07e-13

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: 63.66  E-value: 2.07e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1752980735  88 TYTVQPGDSLSLIASKYNTTYQKIMQLNGL-NNFFIYPGQKLKV 130
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
88-130 5.42e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.77  E-value: 5.42e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1752980735   88 TYTVQPGDSLSLIASKYNTTYQKIMQLNG-LNNFFIYPGQKLKV 130
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 31-70 8.69e-04

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: 36.70  E-value: 8.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1752980735  31 VKAGESVWSISHKYGMSIARLKSLNGLKSN--LIFPNQVLKV 70
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLSNpnLIYPGMKIKI 42
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
208-323 1.17e-39

Surface antigen [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 135.89  E-value: 1.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 208 YRTPIFSHSNLYTWGQCTWHVFNRRAAIGKGISTYWWNANNWDNAAAADGYTINYTPTVGSIAQTDI---GYYGHVAFVE 284
Cdd:COG3942    10 YPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTPgvaGPYGHVAVVE 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1752980735 285 RVNSDGSILVSEMNYSAsPGIMTYRTIPSYQVSSYRYIH 323
Cdd:COG3942    90 SVNSDGSILVSEMNWGG-PGIYSTRTISAGNASSYGFIH 127
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
26-196 2.05e-33

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 129.43  E-value: 2.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  26 ATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKVS---------------GSSKSTANRTANTSSSTYT 90
Cdd:PRK06347  330 AKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSagsttsdtntskpstGTSTSKPSTGTSTNAKVYT 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  91 VQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTG--TAAKNNTKPSQSSKSS-----------IYTVQPGDS 157
Cdd:PRK06347  410 VVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAgsTSNTNTSKPSTNTNTSkpstntntnakVYTVAKGDS 489

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1752980735 158 LSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGTAS 196
Cdd:PRK06347  490 LWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGST 528
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
26-191 1.24e-32

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 127.12  E-value: 1.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  26 ATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKVSGSSKSTANRT--------------ANTSSSTYTV 91
Cdd:PRK06347  405 AKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSkpstntntskpstnTNTNAKVYTV 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  92 QPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGTAAKNNT---KPSQSSKSS----IYTVQPGDSLSLIASK 164
Cdd:PRK06347  485 AKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTntaKPSTNKPSNstvkTYTVKKGDSLWAISRQ 564

                         170       180
                  ....*....|....*....|....*..
gi 1752980735 165 YNTTYQKIMQLNGLNNFFIYPGQKLKV 191
Cdd:PRK06347  565 YKTTVDNIKAWNKLTSNMIHVGQKLTI 591
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 45-189 2.46e-18

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 85.17  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  45 GMSIARLKSLN-GLKSNLIFPN------------QVLKVSGSSKSTAN--RTA---NT--SSSTYTVQPGDSLSLIASKY 104
Cdd:PRK10783  282 GMSLTKLKTFNaGYKRSTTAPSgphyimvpkkhaDQLRESLASGEIAAvqSTLvadNTplNSRSYKVRSGDTLSGIASRL 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 105 NTTYQKIMQLNGLNNFFIYPGQKLKVtGTAAKNNTKPSqSSKSSIYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIY 184
Cdd:PRK10783  362 NVSTKDLQQWNNLRGSKLKVGQTLTI-GAGSSAQRLAN-NSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQ 439


                  ....*
gi 1752980735 185 PGQKL 189
Cdd:PRK10783  440 PGDKL 444
PRK08581 PRK08581
amidase domain-containing protein;
219-322 4.51e-18

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 84.84  E-value: 4.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 219 YTWGQCTWHVFNRRAAIGKGISTYWWNANNWDNAAAADGYTINYTPTVGSIAQTDIG------YYGHVAFVERVNSDGSI 292
Cdd:PRK08581  508 YPHGQCTWYVYNRMKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVVFEAGqagadqHYGHVAFVEKVNSDGSI 587

                          90       100       110
                  ....*....|....*....|....*....|
gi 1752980735 293 LVSEMNYSASpGIMTYRTIPSYQVSSYRYI 322
Cdd:PRK08581  588 VISESNVKGL-GIISYRTIDAAAAEELSYI 616
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
42-194 8.77e-17

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 76.29  E-value: 8.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  42 HKYGMSIARLKSLNGLKSNLIFPNQVLKVSGSSKSTANRTANTSSSTYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFF 121
Cdd:COG1388     5 ALSANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAA 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752980735 122 IYPGQKlKVTGTAAKNNTKPSQSSKSSIYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGT 194
Cdd:COG1388    85 RYTVKS-GDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 89-131 7.74e-15

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: 67.42  E-value: 7.74e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1752980735  89 YTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVT 131
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 150-192 7.74e-15

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: 67.42  E-value: 7.74e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1752980735 150 YTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVT 192
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 26-128 8.56e-15

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 74.77  E-value: 8.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  26 ATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKVsGSSKSTANRTANTSSSTYTVQPGDSLSLIASKYN 105
Cdd:PRK10783  343 SRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI-GAGSSAQRLANNSDSITYRVRKGDSLSSIAKRHG 421

                          90       100
                  ....*....|....*....|...
gi 1752980735 106 TTYQKIMQLNGLNNFFIYPGQKL 128
Cdd:PRK10783  422 VNIKDVMRWNSDTAKNLQPGDKL 444
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
22-73 3.26e-14

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 69.35  E-value: 3.26e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1752980735  22 QAEAATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKVSGS 73
Cdd:COG1388   105 AAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 217-298 4.66e-14

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 66.68  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 217 NLYTWGQCTWHVFNRRAAIGKgistYWWNANNWDNAAAADGYTINYTPTVGSIAQTDIG----YYGHVAFVERVNsDGSI 292
Cdd:pfam05257   3 NGYPWGQCTWFVYWRVAQLGI----YLGNAGDWADAAAGAYKVGSTTPKVGDIVVFDPGgggaSYGHVAIVEKVN-DGSI 77


                  ....*.
gi 1752980735 293 LVSEMN 298
Cdd:pfam05257  78 TVSEQN 83
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 88-130 2.07e-13

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: 63.66  E-value: 2.07e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1752980735  88 TYTVQPGDSLSLIASKYNTTYQKIMQLNGL-NNFFIYPGQKLKV 130
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 149-191 4.86e-13

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: 62.50  E-value: 4.86e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1752980735 149 IYTVQPGDSLSLIASKYNTTYQKIMQLNGL-NNFFIYPGQKLKV 191
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 29-70 3.37e-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: 60.10  E-value: 3.37e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1752980735  29 HTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKV 70
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
LysM smart00257
Lysin motif;
88-130 5.42e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 59.77  E-value: 5.42e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1752980735   88 TYTVQPGDSLSLIASKYNTTYQKIMQLNG-LNNFFIYPGQKLKV 130
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
149-191 1.33e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 58.61  E-value: 1.33e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1752980735  149 IYTVQPGDSLSLIASKYNTTYQKIMQLNG-LNNFFIYPGQKLKV 191
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 27-70 4.56e-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: 57.11  E-value: 4.56e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1752980735  27 TTHTVKAGESVWSISHKYGMSIARLKSLNGLKS-NLIFPNQVLKV 70
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
28-70 1.24e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 55.91  E-value: 1.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1752980735   28 THTVKAGESVWSISHKYGMSIARLKSLNG-LKSNLIFPNQVLKV 70
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 130-191 3.62e-10

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: 58.09  E-value: 3.62e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752980735 130 VTGTAAKNNTKPSQSSKSSIYTVQPGDSLSLIASKY---NTTYQKIMQLN--GLNNF-FIYPGQKLKV 191
Cdd:COG1652    92 TVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPdLIYPGQVLRI 159
PRK13914 PRK13914
invasion associated endopeptidase;
1-195 4.23e-10

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 60.59  E-value: 4.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735   1 MKKKYMAAIIGTsALSTVFAHQAEAATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKVsgSSKSTANR 80
Cdd:PRK13914    3 MKKATIAATAGI-AVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV--NEVAAAEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735  81 TANTSSSTY---------------TVQPGDSLSLIASKYNtTYQKIMQLNGLNNFF-------------IYPGQKLKVTG 132
Cdd:PRK13914   80 TEKSVSATWlnvrsgagvdnsiitSIKGGTKVTVETTESN-GWHKITYNDGKTGFVngkyltdkvtstpVAPTQEVKKET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 133 T--------------------------AAKNNTKPSQSSKSSIYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPG 186
Cdd:PRK13914  159 TtqqaapaaetktevkqttqattpapkVAETKETPVVDQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVG 238


                  ....*....
gi 1752980735 187 QKLKVTGTA 195
Cdd:PRK13914  239 QKLAIKQTA 247
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 74-130 6.73e-10

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: 57.32  E-value: 6.73e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752980735  74 SKSTANRTANTSSSTYTVQPGDSLSLIASKY---NTTYQKIMQLN--GLNNF-FIYPGQKLKV 130
Cdd:COG1652    97 AAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPdLIYPGQVLRI 159
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
133-196 6.46e-08

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 53.93  E-value: 6.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752980735 133 TAAKNNTKPSQSSKSSIYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGTAS 196
Cdd:PRK06347  316 GNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGST 379
PRK13914 PRK13914
invasion associated endopeptidase;
26-78 7.60e-08

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 53.65  E-value: 7.60e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1752980735  26 ATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKVSGSSKSTA 78
Cdd:PRK13914  199 ATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTAT 251
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 125-197 2.53e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 51.66  E-value: 2.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752980735 125 GQKLKVTGTAAKNNTkpsqSSKSSIYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGTASG 197
Cdd:PRK10783  325 GEIAAVQSTLVADNT----PLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSA 393
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 3-70 4.81e-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: 46.15  E-value: 4.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752980735   3 KKYMAAIIGTSALSTVFAHQAEAATTHTVKAGESVWSISHKY---GMSIARLKSLN--GLKS-NLIFPNQVLKV 70
Cdd:COG1652    86 KLSPAVTVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNpDLIYPGQVLRI 159
PRK13914 PRK13914
invasion associated endopeptidase;
83-147 3.68e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 45.18  E-value: 3.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752980735  83 NTSSSTYTVQPGDSLSLIASKYNTTYQKIMQLNGLNNFFIYPGQKLKVTGTAakNNTKPSQSSKS 147
Cdd:PRK13914  196 DQNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTA--NTATPKAEVKT 258
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
25-70 1.89e-04

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 43.14  E-value: 1.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1752980735  25 AATTHTVKAGESVWSISHKYGMSIARLKSLNGLKSNLIFPNQVLKV 70
Cdd:PRK06347  546 TVKTYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 130-191 3.11e-04

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 40.28  E-value: 3.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752980735 130 VTGTAAKNN--TKPSQSSKSSIYTVQPGDSLSLIASKY--NTT-YQKIMQLNG--LNNF-FIYPGQKLKV 191
Cdd:PRK11198   76 IQGIASVDDqvKVATPAPESQFYTVKSGDTLSAIAKKVygNANkYNKIFEANKpmLKSPdKIYPGQVLRI 145
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 150-197 3.26e-04

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


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 41.96  E-value: 3.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1752980735 150 YTVQPGDSLSLIASKYN---TTYQKIMQLNGLNNFF--IYPGQKLKVTGTASG 197
Cdd:COG3061    72 YTVQSGDTLSQIFRRLGlsaSDLYALLAAEGDAKPLsrLKPGQELRFQLDADG 124
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 88-131 3.96e-04

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


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 41.96  E-value: 3.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1752980735  88 TYTVQPGDSLSLIASKYN---TTYQKIMQLNGLNNFF--IYPGQKLKVT 131
Cdd:COG3061    71 EYTVQSGDTLSQIFRRLGlsaSDLYALLAAEGDAKPLsrLKPGQELRFQ 119
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 31-70 8.69e-04

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: 36.70  E-value: 8.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1752980735  31 VKAGESVWSISHKYGMSIARLKSLNGLKSN--LIFPNQVLKV 70
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLSNpnLIYPGMKIKI 42
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 81-130 9.93e-04

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 38.74  E-value: 9.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1752980735  81 TANTSSSTYTVQPGDSLSLIASKY--NTT-YQKIMQLNG--LNNF-FIYPGQKLKV 130
Cdd:PRK11198   90 TPAPESQFYTVKSGDTLSAIAKKVygNANkYNKIFEANKpmLKSPdKIYPGQVLRI 145
 
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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