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Conserved domains on  [gi|1750355294|gb|KAA8434889|]
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LysM peptidoglycan-binding domain-containing protein [Weissella paramesenteroides]

Protein Classification

LysM peptidoglycan-binding domain-containing protein( domain architecture ID 10061503)

LysM peptidoglycan-binding domain-containing protein may bind N-acetylglucosamine in carbohydrates such as chitin, chitio-oligosaccharides and peptidoglycan

CATH:  3.10.350.10
Gene Ontology:  GO:0097367
PubMed:  18430080|24652063
SCOP:  4000905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 90-130 1.73e-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: 49.79  E-value: 1.73e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1750355294  90 VAAGETGYAIATKYGLSVDELQSLNPDVDVNNLREGETLTI 130
Cdd:cd00118     5 VKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
14-131 1.66e-07

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


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 47.40  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750355294  14 IILVGYVAIFLIGFFIPIAYDSVTHKDNQTDMAADAASDSSKQKQKSKPKLATSKKAAVSAKSTKSHATAALSKIEVAAG 93
Cdd:COG1388    38 LAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKG 117

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1750355294  94 ETGYAIATKYGLSVDELQSLNPdVDVNNLREGETLTIK 131
Cdd:COG1388   118 DTLWSIARRYGVSVEELKRWNG-LSSDTIRPGQKLKIP 154
 
Name Accession Description Interval E-value
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 90-130 1.73e-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: 49.79  E-value: 1.73e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1750355294  90 VAAGETGYAIATKYGLSVDELQSLNPDVDVNNLREGETLTI 130
Cdd:cd00118     5 VKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
87-130 6.44e-08

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 45.90  E-value: 6.44e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1750355294   87 KIEVAAGETGYAIATKYGLSVDELQSLNPDVDVNNLREGETLTI 130
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
14-131 1.66e-07

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 47.40  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750355294  14 IILVGYVAIFLIGFFIPIAYDSVTHKDNQTDMAADAASDSSKQKQKSKPKLATSKKAAVSAKSTKSHATAALSKIEVAAG 93
Cdd:COG1388    38 LAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKG 117

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1750355294  94 ETGYAIATKYGLSVDELQSLNPdVDVNNLREGETLTIK 131
Cdd:COG1388   118 DTLWSIARRYGVSVEELKRWNG-LSSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 88-131 1.29e-05

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: 39.69  E-value: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1750355294  88 IEVAAGETGYAIATKYGLSVDELQSLNpDVDVNNLREGETLTIK 131
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPNLYVGQKLKIP 43
PRK13914 PRK13914
invasion associated endopeptidase;
30-131 6.53e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 40.94  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750355294  30 PIAYDSVTHKDNQTDMAADAASDS-----SKQKQKSKPKLATSKKAAVSAKSTKSHAtaalskieVAAGETGYAIATKYG 104
Cdd:PRK13914  147 PVAPTQEVKKETTTQQAAPAAETKtevkqTTQATTPAPKVAETKETPVVDQNATTHA--------VKSGDTIWALSVKYG 218

                          90       100
                  ....*....|....*....|....*..
gi 1750355294 105 LSVDELQSLNpDVDVNNLREGETLTIK 131
Cdd:PRK13914  219 VSVQDIMSWN-NLSSSSIYVGQKLAIK 244
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 64-130 3.17e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 38.95  E-value: 3.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1750355294  64 LATSKKAAVSAKSTKSHATAALSKIEVAAGETGYAIATKYGLSVDELQSLNpDVDVNNLREGETLTI 130
Cdd:PRK10783  322 LASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWN-NLRGSKLKVGQTLTI 387
 
Name Accession Description Interval E-value
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 90-130 1.73e-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: 49.79  E-value: 1.73e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1750355294  90 VAAGETGYAIATKYGLSVDELQSLNPDVDVNNLREGETLTI 130
Cdd:cd00118     5 VKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
87-130 6.44e-08

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 45.90  E-value: 6.44e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1750355294   87 KIEVAAGETGYAIATKYGLSVDELQSLNPDVDVNNLREGETLTI 130
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
14-131 1.66e-07

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 47.40  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750355294  14 IILVGYVAIFLIGFFIPIAYDSVTHKDNQTDMAADAASDSSKQKQKSKPKLATSKKAAVSAKSTKSHATAALSKIEVAAG 93
Cdd:COG1388    38 LAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPVTYTVKKG 117

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1750355294  94 ETGYAIATKYGLSVDELQSLNPdVDVNNLREGETLTIK 131
Cdd:COG1388   118 DTLWSIARRYGVSVEELKRWNG-LSSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 88-131 1.29e-05

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: 39.69  E-value: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1750355294  88 IEVAAGETGYAIATKYGLSVDELQSLNpDVDVNNLREGETLTIK 131
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPNLYVGQKLKIP 43
PRK13914 PRK13914
invasion associated endopeptidase;
30-131 6.53e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 40.94  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750355294  30 PIAYDSVTHKDNQTDMAADAASDS-----SKQKQKSKPKLATSKKAAVSAKSTKSHAtaalskieVAAGETGYAIATKYG 104
Cdd:PRK13914  147 PVAPTQEVKKETTTQQAAPAAETKtevkqTTQATTPAPKVAETKETPVVDQNATTHA--------VKSGDTIWALSVKYG 218

                          90       100
                  ....*....|....*....|....*..
gi 1750355294 105 LSVDELQSLNpDVDVNNLREGETLTIK 131
Cdd:PRK13914  219 VSVQDIMSWN-NLSSSSIYVGQKLAIK 244
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 64-130 3.17e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 38.95  E-value: 3.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1750355294  64 LATSKKAAVSAKSTKSHATAALSKIEVAAGETGYAIATKYGLSVDELQSLNpDVDVNNLREGETLTI 130
Cdd:PRK10783  322 LASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWN-NLRGSKLKVGQTLTI 387
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 1-131 5.14e-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: 35.41  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750355294   1 MKTKK--PSRIKYWIIILVgyvAIFLIGFFIPiaydsvtHKDNQTDMAADAASDSSKQKQKSKPKLATSKKAAVSAKSTK 78
Cdd:COG3061     1 MGRMNplPRKHRRLLGLLS---ALLLLALLLP-------SPDASASRVSQPLVPLALTAEADAPAAAAPAAPAAPEGEWQ 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1750355294  79 SHataalskiEVAAGETGYAIATKYGLSVDELQSL--NPDVD--VNNLREGETLTIK 131
Cdd:COG3061    71 EY--------TVQSGDTLSQIFRRLGLSASDLYALlaAEGDAkpLSRLKPGQELRFQ 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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