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Conserved domains on  [gi|686156288|ref|WP_031788030|]
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autolysin/adhesin Aaa [Staphylococcus argenteus]

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];
211-335 2.78e-37

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


:

Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 130.11  E-value: 2.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 211 GSATTTNSGYRTPIFNHQNLYTWGQCTYHVFNRRAEIGKGISTYWWNANNWDNAAAADGYTIDNRPTVGSIAQTD---VG 287
Cdd:COG3942    1 ARAASLGDGYPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 686156288 288 YYGHVMFVERVNNDGSILVSEMNYSaAPGILTYRTVPAYQVNNYRYIH 335
Cdd:COG3942   81 PYGHVAVVESVNSDGSILVSEMNWG-GPGIYSTRTISAGNASSYGFIH 127
PRK06347 super family cl32140
1,4-beta-N-acetylmuramoylhydrolase;
31-218 2.80e-30

1,4-beta-N-acetylmuramoylhydrolase;


The actual alignment was detected with superfamily member PRK06347:

Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 120.95  E-value: 2.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  31 VQPGESVWAISNKYGISIAKLKSLNGLTSNLIFPNQVLKVSGSSNSASNSSR-----------PSTNSGGGSYYTVQAGD 99
Cdd:PRK06347 335 VVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSkpstgtstskpSTGTSTNAKVYTVVKGD 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 100 SLSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKVSGTASSSNSTS-------NSSRPSTNSGGGSYYTVQAGDSLSLIA 172
Cdd:PRK06347 415 SLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSkpstntnTSKPSTNTNTNAKVYTVAKGDSLWRIA 494

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 686156288 173 SKYGTTYQKIMSLNGLNNFFIYPGQKLKVTGTASTSNSGSATTTNS 218
Cdd:PRK06347 495 NNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTN 540
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
211-335 2.78e-37

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


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 130.11  E-value: 2.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 211 GSATTTNSGYRTPIFNHQNLYTWGQCTYHVFNRRAEIGKGISTYWWNANNWDNAAAADGYTIDNRPTVGSIAQTD---VG 287
Cdd:COG3942    1 ARAASLGDGYPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 686156288 288 YYGHVMFVERVNNDGSILVSEMNYSaAPGILTYRTVPAYQVNNYRYIH 335
Cdd:COG3942   81 PYGHVAVVESVNSDGSILVSEMNWG-GPGIYSTRTISAGNASSYGFIH 127
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
31-218 2.80e-30

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 120.95  E-value: 2.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  31 VQPGESVWAISNKYGISIAKLKSLNGLTSNLIFPNQVLKVSGSSNSASNSSR-----------PSTNSGGGSYYTVQAGD 99
Cdd:PRK06347 335 VVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSkpstgtstskpSTGTSTNAKVYTVVKGD 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 100 SLSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKVSGTASSSNSTS-------NSSRPSTNSGGGSYYTVQAGDSLSLIA 172
Cdd:PRK06347 415 SLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSkpstntnTSKPSTNTNTNAKVYTVAKGDSLWRIA 494

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 686156288 173 SKYGTTYQKIMSLNGLNNFFIYPGQKLKVTGTASTSNSGSATTTNS 218
Cdd:PRK06347 495 NNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTN 540
PRK08581 PRK08581
amidase domain-containing protein;
208-325 6.35e-16

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 78.68  E-value: 6.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 208 SNSGSATTTNSGYrtPIFNHQN---LYTWGQCTYHVFNRRAEIGKGISTYWWNANNWDNAAAADGYTIDNRPTVGSIAQT 284
Cdd:PRK08581 484 SSIKDYDDSSSEF--KPFREYSgssPYPHGQCTWYVYNRMKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVVF 561

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 686156288 285 DVG------YYGHVMFVERVNNDGSILVSEMNYSAApGILTYRTVPA 325
Cdd:PRK08581 562 EAGqagadqHYGHVAFVEKVNSDGSIVISESNVKGL-GIISYRTIDA 607
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
85-134 5.81e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 71.28  E-value: 5.81e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 686156288  85 TNSGGGSYYTVQAGDSLSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKV 134
Cdd:COG1388  104 AAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 160-202 2.36e-14

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: 66.27  E-value: 2.36e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 686156288  160 YTVQAGDSLSLIASKYGTTYQKIMSLNGLNNFFIYPGQKLKVT 202
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 92-134 1.46e-12

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


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 61.35  E-value: 1.46e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 686156288  92 YYTVQAGDSLSLIASKYGTTYQNIMRLNGL-NNFFIYPGQKLKV 134
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
159-201 1.59e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 58.23  E-value: 1.59e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 686156288   159 YYTVQAGDSLSLIASKYGTTYQKIMSLNG-LNNFFIYPGQKLKV 201
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 229-310 3.28e-10

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: 55.89  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  229 NLYTWGQCTYHVFNRRAEIGKgistYWWNANNWDNAAAADGYTIDNRPTVGSIAQTDVG----YYGHVMFVERVnNDGSI 304
Cdd:pfam05257   3 NGYPWGQCTWFVYWRVAQLGI----YLGNAGDWADAAAGAYKVGSTTPKVGDIVVFDPGgggaSYGHVAIVEKV-NDGSI 77


                  ....*.
gi 686156288  305 LVSEMN 310
Cdd:pfam05257  78 TVSEQN 83
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 162-201 2.21e-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: 38.24  E-value: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 686156288  162 VQAGDSLSLIASKYGTTYQKIMSLNGL--NNFFIYPGQKLKV 201
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQlsNPNLIYPGMKIKI 42
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
211-335 2.78e-37

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


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 130.11  E-value: 2.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 211 GSATTTNSGYRTPIFNHQNLYTWGQCTYHVFNRRAEIGKGISTYWWNANNWDNAAAADGYTIDNRPTVGSIAQTD---VG 287
Cdd:COG3942    1 ARAASLGDGYPPNVVDPWNGYPYGQCTWYAAWRRAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 686156288 288 YYGHVMFVERVNNDGSILVSEMNYSaAPGILTYRTVPAYQVNNYRYIH 335
Cdd:COG3942   81 PYGHVAVVESVNSDGSILVSEMNWG-GPGIYSTRTISAGNASSYGFIH 127
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
31-218 2.80e-30

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 120.95  E-value: 2.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  31 VQPGESVWAISNKYGISIAKLKSLNGLTSNLIFPNQVLKVSGSSNSASNSSR-----------PSTNSGGGSYYTVQAGD 99
Cdd:PRK06347 335 VVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSkpstgtstskpSTGTSTNAKVYTVVKGD 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 100 SLSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKVSGTASSSNSTS-------NSSRPSTNSGGGSYYTVQAGDSLSLIA 172
Cdd:PRK06347 415 SLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSkpstntnTSKPSTNTNTNAKVYTVAKGDSLWRIA 494

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 686156288 173 SKYGTTYQKIMSLNGLNNFFIYPGQKLKVTGTASTSNSGSATTTNS 218
Cdd:PRK06347 495 NNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTN 540
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
31-201 6.13e-26

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 108.24  E-value: 6.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  31 VQPGESVWAISNKYGISIAKLKSLNGLTSNLIFPNQVLKVSGSSNSASNSSRPSTN----------SGGGSYYTVQAGDS 100
Cdd:PRK06347 410 VVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNtntskpstntNTNAKVYTVAKGDS 489

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 101 LSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKVSGTASSSNSTSNSSRPSTNSGGGS-YYTVQAGDSLSLIASKYGTTY 179
Cdd:PRK06347 490 LWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTNKPSNSTVkTYTVKKGDSLWAISRQYKTTV 569

                        170       180
                 ....*....|....*....|..
gi 686156288 180 QKIMSLNGLNNFFIYPGQKLKV 201
Cdd:PRK06347 570 DNIKAWNKLTSNMIHVGQKLTI 591
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
86-223 3.57e-20

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 91.29  E-value: 3.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  86 NSGGGSYYTVQAGDSLSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKVSGTASSSNSTSNSSRPSTNSGGGS------- 158
Cdd:PRK06347 326 NTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKPSTGTSTSKPStgtstna 405

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686156288 159 -YYTVQAGDSLSLIASKYGTTYQKIMSLNGLNNFFIYPGQKLKVTGTASTSNSGSATTTNSGYRTP 223
Cdd:PRK06347 406 kVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNTNTSKP 471
PRK08581 PRK08581
amidase domain-containing protein;
208-325 6.35e-16

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 78.68  E-value: 6.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 208 SNSGSATTTNSGYrtPIFNHQN---LYTWGQCTYHVFNRRAEIGKGISTYWWNANNWDNAAAADGYTIDNRPTVGSIAQT 284
Cdd:PRK08581 484 SSIKDYDDSSSEF--KPFREYSgssPYPHGQCTWYVYNRMKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVVF 561

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 686156288 285 DVG------YYGHVMFVERVNNDGSILVSEMNYSAApGILTYRTVPA 325
Cdd:PRK08581 562 EAGqagadqHYGHVAFVEKVNSDGSIVISESNVKGL-GIISYRTIDA 607
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
85-134 5.81e-15

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 71.28  E-value: 5.81e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 686156288  85 TNSGGGSYYTVQAGDSLSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKV 134
Cdd:COG1388  104 AAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
153-204 1.62e-14

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 70.12  E-value: 1.62e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 686156288 153 NSGGGSYYTVQAGDSLSLIASKYGTTYQKIMSLNGLNNFFIYPGQKLKVTGT 204
Cdd:COG1388  105 AAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 160-202 2.36e-14

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: 66.27  E-value: 2.36e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 686156288  160 YTVQAGDSLSLIASKYGTTYQKIMSLNGLNNFFIYPGQKLKVT 202
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 ...
 93-134 5.11e-14

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


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 65.11  E-value: 5.11e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 686156288   93 YTVQAGDSLSLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKV 134
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 45-199 1.53e-13

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 70.92  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  45 GISIAKLKSLN-GLTSNLIFPN----------------------QVLKVsgssnsaSNSSRPSTNSGGGSYYTVQAGDSL 101
Cdd:PRK10783 282 GMSLTKLKTFNaGYKRSTTAPSgphyimvpkkhadqlreslasgEIAAV-------QSTLVADNTPLNSRSYKVRSGDTL 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 102 SLIASKYGTTYQNIMRLNGLNNFFIYPGQKLKVsgtasssnSTSNSSRPSTNSGGGSYYTVQAGDSLSLIASKYGTTYQK 181
Cdd:PRK10783 355 SGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI--------GAGSSAQRLANNSDSITYRVRKGDSLSSIAKRHGVNIKD 426

                        170
                 ....*....|....*...
gi 686156288 182 IMSLNGLNNFFIYPGQKL 199
Cdd:PRK10783 427 VMRWNSDTAKNLQPGDKL 444
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 92-134 1.46e-12

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


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 61.35  E-value: 1.46e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 686156288  92 YYTVQAGDSLSLIASKYGTTYQNIMRLNGL-NNFFIYPGQKLKV 134
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 159-201 2.15e-12

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


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 60.96  E-value: 2.15e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 686156288 159 YYTVQAGDSLSLIASKYGTTYQKIMSLNGL-NNFFIYPGQKLKV 201
Cdd:cd00118    2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 31-132 2.30e-12

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 67.45  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  31 VQPGESVWAISNKYGISIAKLKSLNGLTSNLIFPNQVLKVsgssnSASNSSRPSTNSGGGSYYTVQAGDSLSLIASKYGT 110
Cdd:PRK10783 348 VRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI-----GAGSSAQRLANNSDSITYRVRKGDSLSSIAKRHGV 422

                         90       100
                 ....*....|....*....|..
gi 686156288 111 TYQNIMRLNGLNNFFIYPGQKL 132
Cdd:PRK10783 423 NIKDVMRWNSDTAKNLQPGDKL 444
LysM smart00257
Lysin motif;
159-201 1.59e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 58.23  E-value: 1.59e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 686156288   159 YYTVQAGDSLSLIASKYGTTYQKIMSLNG-LNNFFIYPGQKLKV 201
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM smart00257
Lysin motif;
92-134 3.51e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 57.46  E-value: 3.51e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 686156288    92 YYTVQAGDSLSLIASKYGTTYQNIMRLNG-LNNFFIYPGQKLKV 134
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 31-70 3.88e-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: 57.41  E-value: 3.88e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 686156288   31 VQPGESVWAISNKYGISIAKLKSLNGLTSNLIFPNQVLKV 70
Cdd:pfam01476   3 VKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 229-310 3.28e-10

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: 55.89  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  229 NLYTWGQCTYHVFNRRAEIGKgistYWWNANNWDNAAAADGYTIDNRPTVGSIAQTDVG----YYGHVMFVERVnNDGSI 304
Cdd:pfam05257   3 NGYPWGQCTWFVYWRVAQLGI----YLGNAGDWADAAAGAYKVGSTTPKVGDIVVFDPGgggaSYGHVAIVEKV-NDGSI 77


                  ....*.
gi 686156288  305 LVSEMN 310
Cdd:pfam05257  78 TVSEQN 83
PRK13914 PRK13914
invasion associated endopeptidase;
1-218 2.95e-09

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 57.89  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288   1 MQKKVIAAIIGTsAISAVAATQANAATTHTVQPGESVWAISNKYGISIAKLKSLNGLTSNLIFPNQVLKVSGSSNSASNS 80
Cdd:PRK13914   3 MKKATIAATAGI-AVTAFAAPTIASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAEKTE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288  81 SRPS-----------------TNSGGGSYYTVQAGDSLSLIASKYG---TTYQNIMRL-NGLNNFFIYPGQKLKVSGTAS 139
Cdd:PRK13914  82 KSVSatwlnvrsgagvdnsiiTSIKGGTKVTVETTESNGWHKITYNdgkTGFVNGKYLtDKVTSTPVAPTQEVKKETTTQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686156288 140 SSNSTSNSSRPSTNSG--------------------GGSYYTVQAGDSLSLIASKYGTTYQKIMSLNGLNNFFIYPGQKL 199
Cdd:PRK13914 162 QAAPAAETKTEVKQTTqattpapkvaetketpvvdqNATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKL 241

                        250
                 ....*....|....*....
gi 686156288 200 KVTGTASTSNSGSATTTNS 218
Cdd:PRK13914 242 AIKQTANTATPKAEVKTEA 260
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 85-134 4.07e-09

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: 55.01  E-value: 4.07e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 686156288  85 TNSGGGSYYTVQAGDSLSLIASKY---GTTYQNIMRLN--GLNNF-FIYPGQKLKV 134
Cdd:COG1652  104 LAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPdLIYPGQVLRI 159
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 153-201 4.27e-09

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: 55.01  E-value: 4.27e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 686156288 153 NSGGGSYYTVQAGDSLSLIASKY---GTTYQKIMSLN--GLNNF-FIYPGQKLKV 201
Cdd:COG1652  105 APDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPdLIYPGQVLRI 159
LysM smart00257
Lysin motif;
31-70 5.00e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 51.29  E-value: 5.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 686156288    31 VQPGESVWAISNKYGISIAKLKSLNG-LTSNLIFPNQVLKV 70
Cdd:smart00257   4 VKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 31-70 8.20e-09

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: 50.95  E-value: 8.20e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 686156288  31 VQPGESVWAISNKYGISIAKLKSLNGLTS-NLIFPNQVLKV 70
Cdd:cd00118    5 VKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 153-218 5.08e-06

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 47.81  E-value: 5.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 686156288 153 NSGGGSYYTVQAGDSLSLIASKYGTTYQKIMSLNGLNNFFIYPGQKLKVTGTASTSNsgSATTTNS 218
Cdd:PRK10783 339 TPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQR--LANNSDS 402
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 159-201 9.61e-05

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 41.82  E-value: 9.61e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 686156288 159 YYTVQAGDSLSLIASKY---GTTYQKIMSLNG--LNNF-FIYPGQKLKV 201
Cdd:PRK11198  97 FYTVKSGDTLSAIAKKVygnANKYNKIFEANKpmLKSPdKIYPGQVLRI 145
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 162-201 2.21e-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: 38.24  E-value: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 686156288  162 VQAGDSLSLIASKYGTTYQKIMSLNGL--NNFFIYPGQKLKV 201
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQlsNPNLIYPGMKIKI 42
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 95-134 4.66e-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: 37.47  E-value: 4.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 686156288   95 VQAGDSLSLIASKYGTTYQNIMRLNGL--NNFFIYPGQKLKV 134
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQlsNPNLIYPGMKIKI 42
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 92-134 1.26e-03

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 38.74  E-value: 1.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 686156288  92 YYTVQAGDSLSLIASKY---GTTYQNIMRLNG--LNNF-FIYPGQKLKV 134
Cdd:PRK11198  97 FYTVKSGDTLSAIAKKVygnANKYNKIFEANKpmLKSPdKIYPGQVLRI 145
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 160-202 8.33e-03

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: 37.72  E-value: 8.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 686156288 160 YTVQAGDSLSLIASKYG---TTYQKIMSLNGLNNFF--IYPGQKLKVT 202
Cdd:COG3061   72 YTVQSGDTLSQIFRRLGlsaSDLYALLAAEGDAKPLsrLKPGQELRFQ 119
 
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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