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Conserved domains on  [gi|1046311721|gb|ANV75309|]
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Peptidoglycan-binding lysin domain-containing protein [Acetivibrio thermocellus DSM 2360]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
127-229 4.45e-28

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 103.02  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721 127 VNVAERTLTVYRDGRIYRTYRIALENPASPIPRGTFTVLNKQVDP----------------GVEMGARWIGLSEAGFGIH 190
Cdd:COG1376     3 VDLSEQRLYVYEDGGLVRTYPVSVGRPGFPTPTGTFRVLRKAENPtwtppaempagmpggpDNPLGPYALYLSDGGYGIH 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1046311721 191 GTNTPEFIDVVSTGNSIVMSNEDVSELFNLVPVGTIVTI 229
Cdd:COG1376    83 GTPWPSSIGRNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
LysM smart00257
Lysin motif;
16-58 1.31e-14

Lysin motif;


:

Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 65.54  E-value: 1.31e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1046311721   16 YTIKAGDTLAAIARIYGTTVQDIINANPDIDPYYLRVGQQICI 58
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
74-117 1.28e-09

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: 52.01  E-value: 1.28e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046311721  74 YVVRPEDTLESIAAYFNITPQQLLYSNyGIDPTDLYVDQILCIP 117
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPNLYVGQKLKIP 43
 
Name Accession Description Interval E-value
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
127-229 4.45e-28

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 103.02  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721 127 VNVAERTLTVYRDGRIYRTYRIALENPASPIPRGTFTVLNKQVDP----------------GVEMGARWIGLSEAGFGIH 190
Cdd:COG1376     3 VDLSEQRLYVYEDGGLVRTYPVSVGRPGFPTPTGTFRVLRKAENPtwtppaempagmpggpDNPLGPYALYLSDGGYGIH 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1046311721 191 GTNTPEFIDVVSTGNSIVMSNEDVSELFNLVPVGTIVTI 229
Cdd:COG1376    83 GTPWPSSIGRNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
YkuD_like cd16913
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like ...
127-229 5.14e-20

L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.


Pssm-ID: 341130 [Multi-domain]  Cd Length: 121  Bit Score: 81.97  E-value: 5.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721 127 VNVAERTLTVYRDGRIYRTYRIALENPASPIPRGTFTVLNKQVDP------------GVEMGARWIGLS--EAGFGIHGT 192
Cdd:cd16913     4 VDLSEQRLYLYENGKLVKTYPVSTGKPGTPTPTGTFRITRKVKNPtwtgppsippgpYNPLGPYALRLSgpGSGIGIHGT 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1046311721 193 NTPEFIDVVSTGNSIVMSNEDVSELFNLVPVGTIVTI 229
Cdd:cd16913    84 PWPSSIGRPASHGCIRLSNEDAKELYDWVPVGTPVVI 120
LysM smart00257
Lysin motif;
16-58 1.31e-14

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 65.54  E-value: 1.31e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1046311721   16 YTIKAGDTLAAIARIYGTTVQDIINANPDIDPYYLRVGQQICI 58
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
16-58 7.16e-14

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: 7.16e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1046311721  16 YTIKAGDTLAAIARIYGTTVQDIINANPDIDPYYLRVGQQICI 58
Cdd:cd00118     3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
16-59 1.09e-13

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: 63.18  E-value: 1.09e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046311721  16 YTIKAGDTLAAIARIYGTTVQDIINANpDIDPYYLRVGQQICIP 59
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPNLYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
5-59 2.11e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.50  E-value: 2.11e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046311721   5 YQRQCPTGSVPYTIKAGDTLAAIARIYGTTVQDIINANPdIDPYYLRVGQQICIP 59
Cdd:COG1388   101 YGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNG-LSSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
74-117 1.28e-09

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: 52.01  E-value: 1.28e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046311721  74 YVVRPEDTLESIAAYFNITPQQLLYSNyGIDPTDLYVDQILCIP 117
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPNLYVGQKLKIP 43
YkuD pfam03734
L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. ...
122-229 2.85e-09

L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.


Pssm-ID: 461031 [Multi-domain]  Cd Length: 89  Bit Score: 52.35  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721 122 PVTVNVNVAE-RTLTVYRDGRIYRTYRIALENPASPIPRGTFTVlnkqvdpgvemgarwiglseagFGIHGTNTPEfIDV 200
Cdd:pfam03734   1 DRYIVVDLSEqRLLYLYENGGLVLRYPVSVGRGDGPTPTGTFRI----------------------IYIHDTGTPD-LFG 57
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1046311721 201 VSTGNS---IVMSNEDVSELFNLVPVGTIVTI 229
Cdd:pfam03734  58 LGRRRShgcIRLSNEDAKELYDRVLVGTPVVI 89
LysM smart00257
Lysin motif;
73-116 7.84e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 50.14  E-value: 7.84e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1046311721   73 YYVVRPEDTLESIAAYFNITPQQLLYSNYGIDPTDLYVDQILCI 116
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
73-116 1.37e-07

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: 46.71  E-value: 1.37e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046311721  73 YYVVRPEDTLESIAAYFNITPQQLLYSNYGIDPTDLYVDQILCI 116
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
10-110 2.48e-06

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 47.42  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721  10 PTGSVPYTIKAGDTLAAIARIYGTTVQDIINANpDIDPYYLRVGQ--QICIPLTMQIYPSCPTTNYYVVRPEDTLESIAA 87
Cdd:PRK10783  340 PLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWN-NLRGSKLKVGQtlTIGAGSSAQRLANNSDSITYRVRKGDSLSSIAK 418
                          90       100       110
                  ....*....|....*....|....*....|
gi 1046311721  88 YFNITPQQLLYSNYGID----PTD---LYV 110
Cdd:PRK10783  419 RHGVNIKDVMRWNSDTAknlqPGDkltLFV 448
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
18-59 3.47e-05

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: 40.17  E-value: 3.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1046311721  18 IKAGDTLAAIARIYGTTVQDIINANPDI-DPYYLRVGQQICIP 59
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLsNPNLIYPGMKIKIP 43
nlpD PRK10871
murein hydrolase activator NlpD;
5-56 6.82e-04

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 39.82  E-value: 6.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046311721   5 YQRQ---CPTGSV---PYTIKAGDTLAAIARIYGTTVQDIINANPDIDPYYLRVGQQI 56
Cdd:PRK10871   46 YNRQygnIPKGSYsgsTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTL 103
 
Name Accession Description Interval E-value
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
127-229 4.45e-28

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 103.02  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721 127 VNVAERTLTVYRDGRIYRTYRIALENPASPIPRGTFTVLNKQVDP----------------GVEMGARWIGLSEAGFGIH 190
Cdd:COG1376     3 VDLSEQRLYVYEDGGLVRTYPVSVGRPGFPTPTGTFRVLRKAENPtwtppaempagmpggpDNPLGPYALYLSDGGYGIH 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1046311721 191 GTNTPEFIDVVSTGNSIVMSNEDVSELFNLVPVGTIVTI 229
Cdd:COG1376    83 GTPWPSSIGRNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
YkuD_like cd16913
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like ...
127-229 5.14e-20

L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.


Pssm-ID: 341130 [Multi-domain]  Cd Length: 121  Bit Score: 81.97  E-value: 5.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721 127 VNVAERTLTVYRDGRIYRTYRIALENPASPIPRGTFTVLNKQVDP------------GVEMGARWIGLS--EAGFGIHGT 192
Cdd:cd16913     4 VDLSEQRLYLYENGKLVKTYPVSTGKPGTPTPTGTFRITRKVKNPtwtgppsippgpYNPLGPYALRLSgpGSGIGIHGT 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1046311721 193 NTPEFIDVVSTGNSIVMSNEDVSELFNLVPVGTIVTI 229
Cdd:cd16913    84 PWPSSIGRPASHGCIRLSNEDAKELYDWVPVGTPVVI 120
LysM smart00257
Lysin motif;
16-58 1.31e-14

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 65.54  E-value: 1.31e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1046311721   16 YTIKAGDTLAAIARIYGTTVQDIINANPDIDPYYLRVGQQICI 58
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
16-58 7.16e-14

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: 7.16e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1046311721  16 YTIKAGDTLAAIARIYGTTVQDIINANPDIDPYYLRVGQQICI 58
Cdd:cd00118     3 YTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
16-59 1.09e-13

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: 63.18  E-value: 1.09e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046311721  16 YTIKAGDTLAAIARIYGTTVQDIINANpDIDPYYLRVGQQICIP 59
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPNLYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
5-59 2.11e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 65.50  E-value: 2.11e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046311721   5 YQRQCPTGSVPYTIKAGDTLAAIARIYGTTVQDIINANPdIDPYYLRVGQQICIP 59
Cdd:COG1388   101 YGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNG-LSSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
74-117 1.28e-09

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: 52.01  E-value: 1.28e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046311721  74 YVVRPEDTLESIAAYFNITPQQLLYSNyGIDPTDLYVDQILCIP 117
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPNLYVGQKLKIP 43
YkuD pfam03734
L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. ...
122-229 2.85e-09

L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.


Pssm-ID: 461031 [Multi-domain]  Cd Length: 89  Bit Score: 52.35  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721 122 PVTVNVNVAE-RTLTVYRDGRIYRTYRIALENPASPIPRGTFTVlnkqvdpgvemgarwiglseagFGIHGTNTPEfIDV 200
Cdd:pfam03734   1 DRYIVVDLSEqRLLYLYENGGLVLRYPVSVGRGDGPTPTGTFRI----------------------IYIHDTGTPD-LFG 57
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1046311721 201 VSTGNS---IVMSNEDVSELFNLVPVGTIVTI 229
Cdd:pfam03734  58 LGRRRShgcIRLSNEDAKELYDRVLVGTPVVI 89
LysM smart00257
Lysin motif;
73-116 7.84e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 50.14  E-value: 7.84e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1046311721   73 YYVVRPEDTLESIAAYFNITPQQLLYSNYGIDPTDLYVDQILCI 116
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
10-119 1.58e-08

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 52.40  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721  10 PTGSVPYTIKAGDTLAAIARIYGTtvqdiinanpdidpyylrvgqqicipltmqiyPSCPTTNYYVVRPEDTLESIAAYF 89
Cdd:COG1388    80 AAAAARYTVKSGDTLSGIARRYGA--------------------------------AAAPSPVTYTVKKGDTLWSIARRY 127
                          90       100       110
                  ....*....|....*....|....*....|
gi 1046311721  90 NITPQQLLYSNyGIDPTDLYVDQILCIPVA 119
Cdd:COG1388   128 GVSVEELKRWN-GLSSDTIRPGQKLKIPAS 156
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
73-116 1.37e-07

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: 46.71  E-value: 1.37e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046311721  73 YYVVRPEDTLESIAAYFNITPQQLLYSNYGIDPTDLYVDQILCI 116
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
10-59 7.39e-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: 47.69  E-value: 7.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046311721  10 PTGSVPYTIKAGDTLAAIA-RIYGTTVQ--DIINANPDI--DPYYLRVGQQICIP 59
Cdd:COG1652   106 PDAPKTYTVKPGDTLWGIAkRFYGDPARwpEIAEANRDQikNPDLIYPGQVLRIP 160
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
10-110 2.48e-06

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 47.42  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046311721  10 PTGSVPYTIKAGDTLAAIARIYGTTVQDIINANpDIDPYYLRVGQ--QICIPLTMQIYPSCPTTNYYVVRPEDTLESIAA 87
Cdd:PRK10783  340 PLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWN-NLRGSKLKVGQtlTIGAGSSAQRLANNSDSITYRVRKGDSLSSIAK 418
                          90       100       110
                  ....*....|....*....|....*....|
gi 1046311721  88 YFNITPQQLLYSNYGID----PTD---LYV 110
Cdd:PRK10783  419 RHGVNIKDVMRWNSDTAknlqPGDkltLFV 448
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
18-59 3.47e-05

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: 40.17  E-value: 3.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1046311721  18 IKAGDTLAAIARIYGTTVQDIINANPDI-DPYYLRVGQQICIP 59
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLsNPNLIYPGMKIKIP 43
nlpD PRK10871
murein hydrolase activator NlpD;
5-56 6.82e-04

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 39.82  E-value: 6.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046311721   5 YQRQ---CPTGSV---PYTIKAGDTLAAIARIYGTTVQDIINANPDIDPYYLRVGQQI 56
Cdd:PRK10871   46 YNRQygnIPKGSYsgsTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTL 103
PRK06132 PRK06132
hypothetical protein; Provisional
117-170 9.65e-04

hypothetical protein; Provisional


Pssm-ID: 235709 [Multi-domain]  Cd Length: 359  Bit Score: 39.66  E-value: 9.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046311721 117 PVAPP--PVTVNVNVAERTLTVYRDGRIYRTYRIALENPASPIPRGTFTVLNKQVD 170
Cdd:PRK06132   53 PEAKPqgPLVIVVSLDEQRLYVYDNGILIAVSTVSTGKRGHETPTGVFSILQKDKD 108
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
16-56 1.52e-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: 39.26  E-value: 1.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1046311721  16 YTIKAGDTLAAIARIYG---TTVQDIINANPDIDPY-YLRVGQQI 56
Cdd:COG3061    72 YTVQSGDTLSQIFRRLGlsaSDLYALLAAEGDAKPLsRLKPGQEL 116
 
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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