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Conserved domains on  [gi|1906335194|ref|WP_189104029|]
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M23 family metallopeptidase [Deinococcus knuensis]

Protein Classification

M23 family metallopeptidase( domain architecture ID 11432770)

M23 family metallopeptidase lyses bacterial cell wall peptidoglycans

EC:  3.4.24.-
Gene Ontology:  GO:0046872|GO:0008237
MEROPS:  M23
PubMed:  36386627

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 34-206 6.81e-47

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 152.82  E-value: 6.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  34 ARRQGVSLEALLAKNKSLNPQLALKVGQVLQLPARSGTARVATTMNGGVVRPAGIRVSAVLPVQGRLTSPYSP------- 106
Cdd:COG0739    13 ALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYrrhpvtg 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 107 ---AHLGLDLAAPTGTPFVAARAGRVTESRFDarTGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTG 183
Cdd:COG0739    93 rrrFHKGIDIAAPTGTPVYAAADGTVVFAGWN--GGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTG 170

                         170       180
                  ....*....|....*....|...
gi 1906335194 184 NSTGPHLDFRVMVNGNVINPMGL 206
Cdd:COG0739   171 RSTGPHLHFEVRVNGKPVDPLPF 193
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 34-206 6.81e-47

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 152.82  E-value: 6.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  34 ARRQGVSLEALLAKNKSLNPQLALKVGQVLQLPARSGTARVATTMNGGVVRPAGIRVSAVLPVQGRLTSPYSP------- 106
Cdd:COG0739    13 ALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYrrhpvtg 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 107 ---AHLGLDLAAPTGTPFVAARAGRVTESRFDarTGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTG 183
Cdd:COG0739    93 rrrFHKGIDIAAPTGTPVYAAADGTVVFAGWN--GGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTG 170

                         170       180
                  ....*....|....*....|...
gi 1906335194 184 NSTGPHLDFRVMVNGNVINPMGL 206
Cdd:COG0739   171 RSTGPHLHFEVRVNGKPVDPLPF 193
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 108-203 1.26e-38

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 128.43  E-value: 1.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 108 HLGLDLAAPTGTPFVAARAGRVTESRFDArtGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTGNSTG 187
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFAGWLG--GYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 1906335194 188 PHLDFRVMVNGNVINP 203
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 108-194 2.89e-34

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 116.92  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 108 HLGLDLAAPTGTPFVAARAGRVTESRFDarTGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTGNSTG 187
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD--GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTG 78


                  ....*..
gi 1906335194 188 PHLDFRV 194
Cdd:cd12797    79 PHLHFEI 85
PRK11649 PRK11649
putative peptidase; Provisional
 95-204 2.90e-20

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 87.41  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  95 PVQGRLTspyspAHLGLDLAAPTGTPFVAARAGRVTESRFDARTGWgwTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQ 174
Cdd:PRK11649  305 PVTGRVA-----PHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGN--YVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGD 377

                          90       100       110
                  ....*....|....*....|....*....|
gi 1906335194 175 VIGRVGSTGNSTGPHLDFRVMVNGNVINPM 204
Cdd:PRK11649  378 RIALSGNTGRSTGPHLHYEVWINQQAVNPL 407
LysM smart00257
Lysin motif;
21-65 9.76e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 60.15  E-value: 9.76e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1906335194   21 TVTVKPGDTLYGIARRQGVSLEALLAKNKSLNPQlALKVGQVLQL 65
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPD-NLQVGQKLKI 44
FimV_core TIGR03505
FimV N-terminal domain; This region is found at, or about 200 amino acids from, the N-terminus ...
 28-76 5.85e-03

FimV N-terminal domain; This region is found at, or about 200 amino acids from, the N-terminus of FimV from Pseudomonas aeruginosa, TspA of Neisseria meningitidis, and related proteins. Disruption of FimV blocks twitching motility from type IV pili; Semmler, et al. suggest a role for this family in peptidoglycan layer remodelling required by type IV fimbrial systems. Most but not all members of this protein family have a C-terminal region recognized by TIGR03504. In between is a highly variable, often repeat-filled region rich in the negatively charged amino acids Asp and Glu.


Pssm-ID: 274615 [Multi-domain]  Cd Length: 74  Bit Score: 34.62  E-value: 5.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  28 DTLYGIARR----QGVSLEALLAKNKSLNPQL-------ALKVGQVLQLPARSGTARVAT 76
Cdd:TIGR03505   1 DTLWGIAQRvrpdNSVSLYQMMLALYRANPDAfiggninRLKVGQILRIPSEEEIQAVSP 60
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 34-206 6.81e-47

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 152.82  E-value: 6.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  34 ARRQGVSLEALLAKNKSLNPQLALKVGQVLQLPARSGTARVATTMNGGVVRPAGIRVSAVLPVQGRLTSPYSP------- 106
Cdd:COG0739    13 ALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYrrhpvtg 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 107 ---AHLGLDLAAPTGTPFVAARAGRVTESRFDarTGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTG 183
Cdd:COG0739    93 rrrFHKGIDIAAPTGTPVYAAADGTVVFAGWN--GGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTG 170

                         170       180
                  ....*....|....*....|...
gi 1906335194 184 NSTGPHLDFRVMVNGNVINPMGL 206
Cdd:COG0739   171 RSTGPHLHFEVRVNGKPVDPLPF 193
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 108-203 1.26e-38

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 128.43  E-value: 1.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 108 HLGLDLAAPTGTPFVAARAGRVTESRFDArtGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTGNSTG 187
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFAGWLG--GYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 1906335194 188 PHLDFRVMVNGNVINP 203
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 93-204 6.49e-36

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 124.75  E-value: 6.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  93 VLPVQGRLTSPYSP------------AHLGLDLAAPTGTPFVAARAGRVTESRFDarTGWGWTIVLDHGAGMTTRYSHNS 160
Cdd:COG5821    70 LKPVSGKITREFGEdlvysktlnewrTHTGIDIAAKEGTPVKAAADGVVVEVGKD--PKYGITVVIDHGNGIKTVYANLD 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1906335194 161 AN-LVQVGQTVETGQVIGRVGSTGN---STGPHLDFRVMVNGNVINPM 204
Cdd:COG5821   148 SKiKVKVGQKVKKGQVIGKVGSTALfesSEGPHLHFEVLKNGKPVDPM 195
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 41-204 9.31e-36

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 129.11  E-value: 9.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  41 LEALLAKNKSLNPQLAlKVGQVLQLPARSGTARVATTMNGGVVrpagirvsavLPVQGRLTSPYSPA------HLGLDLA 114
Cdd:COG4942   215 LAELQQEAEELEALIA-RLEAEAAAAAERTPAAGFAALKGKLP----------WPVSGRVVRRFGERdggggrNKGIDIA 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 115 APTGTPFVAARAGRVTESrfDARTGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTGNSTGPHLDFRV 194
Cdd:COG4942   284 APPGAPVRAVADGTVVYA--GWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFEL 361

                         170
                  ....*....|
gi 1906335194 195 MVNGNVINPM 204
Cdd:COG4942   362 RKNGKPVDPL 371
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 108-194 2.89e-34

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 116.92  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 108 HLGLDLAAPTGTPFVAARAGRVTESRFDarTGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTGNSTG 187
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD--GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTG 78


                  ....*..
gi 1906335194 188 PHLDFRV 194
Cdd:cd12797    79 PHLHFEI 85
PRK11649 PRK11649
putative peptidase; Provisional
 95-204 2.90e-20

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 87.41  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  95 PVQGRLTspyspAHLGLDLAAPTGTPFVAARAGRVTESRFDARTGWgwTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQ 174
Cdd:PRK11649  305 PVTGRVA-----PHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGN--YVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGD 377

                          90       100       110
                  ....*....|....*....|....*....|
gi 1906335194 175 VIGRVGSTGNSTGPHLDFRVMVNGNVINPM 204
Cdd:PRK11649  378 RIALSGNTGRSTGPHLHYEVWINQQAVNPL 407
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 91-203 5.86e-17

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 75.80  E-value: 5.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  91 SAVLPVQGRLTSPYSPAHLGLDLAAPTGTPFVAARAGRVTESrfDARTGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTV 170
Cdd:COG5833   103 AFALPVSGKVVESFQENGKGVDIETPGGANVKAVKEGYVIFA--GKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFV 180

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1906335194 171 ETGQVIGRVGSTGNSTGpHLDFRVMVNGNVINP 203
Cdd:COG5833   181 EAGQKIGTVPATEGEEG-TFYFAIKKGGKFIDP 212
PRK11637 PRK11637
AmiB activator; Provisional
 66-203 1.09e-15

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 74.34  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  66 PARSGTARVATTmnGGVVRPAGirvSAVLPVQGRLTSPYSPA---HL---GLDLAAPTGTPFVAARAGRVTESrfDARTG 139
Cdd:PRK11637  286 PTESERSLMSRT--GGLGRPRG---QAFWPVRGPTLHRFGEQlqgELrwkGMVIGASEGTEVKAIADGRVLLA--DWLQG 358

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906335194 140 WGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTGNSTGPHLDFRVMVNGNVINP 203
Cdd:PRK11637  359 YGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNP 422
LysM smart00257
Lysin motif;
21-65 9.76e-13

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 60.15  E-value: 9.76e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1906335194   21 TVTVKPGDTLYGIARRQGVSLEALLAKNKSLNPQlALKVGQVLQL 65
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPD-NLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 21-65 1.34e-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: 59.81  E-value: 1.34e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1906335194  21 TVTVKPGDTLYGIARRQGVSLEALLAKNKSLNPQLaLKVGQVLQL 65
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDC-IYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 22-66 9.62e-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: 57.41  E-value: 9.62e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1906335194  22 VTVKPGDTLYGIARRQGVSLEALLAKNKsLNPQlALKVGQVLQLP 66
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNG-LSSP-NLYVGQKLKIP 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
17-68 1.10e-11

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 60.49  E-value: 1.10e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1906335194  17 STAATVTVKPGDTLYGIARRQGVSLEALLAKNKsLNPQLaLKVGQVLQLPAR 68
Cdd:COG1388   107 PSPVTYTVKKGDTLWSIARRYGVSVEELKRWNG-LSSDT-IRPGQKLKIPAS 156
PRK06148 PRK06148
hypothetical protein; Provisional
 108-192 5.16e-11

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 61.19  E-value: 5.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  108 HLGLDLAAPTGTPFVAARAGRVTESRFDA-RTGWGWTIVLDH----GAGMTTRY---SHNSANLVQVGQTVETGQVIGRV 179
Cdd:PRK06148   441 HLGVDLFAPAGTPVYAPLAGTVRSVEIEAvPLGYGGLVALEHetpgGDPFYTLYghlAHEAVSRLKPGDRLAAGELFGAM 520

                           90
                   ....*....|....*
gi 1906335194  180 GSTGNSTG--PHLDF 192
Cdd:PRK06148   521 GDAHENGGwaPHLHF 535
nlpD PRK10871
murein hydrolase activator NlpD;
18-204 7.02e-11

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 60.23  E-value: 7.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  18 TAATVTVKPGDTLYGIARRQGVSLEALLAKNKSLNPqLALKVGQVLQLPARSGT--------ARVATTMNGGVVRPAGIR 89
Cdd:PRK10871   59 SGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAP-YSLNVGQTLQVGNASGTpitggnaiTQADAAEQGVVIKPAQNS 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  90 VSAV------------------------------------------------------------LPVQGRLTSPYSPA-- 107
Cdd:PRK10871  138 TVAVasqptitysessgeqsankmlpnnkpaattvtapvtaptastteptasstststpistwrWPTDGKVIENFSASeg 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194 108 -HLGLDLAAPTGTPFVAARAGRVTESRfDARTGWGWTIVLDHGAGMTTRYSHNSANLVQVGQTVETGQVIGRVGSTGNST 186
Cdd:PRK10871  218 gNKGIDIAGSKGQAIIATADGRVVYAG-NALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS 296

                         250
                  ....*....|....*...
gi 1906335194 187 gPHLDFRVMVNGNVINPM 204
Cdd:PRK10871  297 -TRLHFEIRYKGKSVNPL 313
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 17-79 9.34e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 48.58  E-value: 9.34e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906335194  17 STAATVTVKPGDTLYGIARRQGVSLEALLAKNkSLNPQlALKVGQVLQLPARSGTARVATTMN 79
Cdd:PRK10783  341 LNSRSYKVRSGDTLSGIASRLNVSTKDLQQWN-NLRGS-KLKVGQTLTIGAGSSAQRLANNSD 401
FimV COG3170
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
17-138 4.32e-06

Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];


Pssm-ID: 442403 [Multi-domain]  Cd Length: 508  Bit Score: 46.33  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  17 STAATVTVKPGDTLYGIARR-----QGVSLEALLAKNKSLNPQL-------ALKVGQVLQLPARSGTARVATTmnggvvr 84
Cdd:COG3170   145 ASGEYYPVRPGDTLWSIAARpvrpsSGVSLDQMMVALYRANPDAfidgninRLKAGAVLRVPAAEEVAALSPA------- 217

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1906335194  85 pagiRVSAVLPVQGRLTSPYSPAHLGLDLAAPTGTPFVAARAGRVTESRFDART 138
Cdd:COG3170   218 ----EARQEVQAQSADWAAYRARLAAAVEPAPAAAAPAAPPAAAAAAGPVPAAA 267
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 17-67 6.10e-05

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: 41.92  E-value: 6.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1906335194  17 STAATVTVKPGDTLYGIARRQ---GVSLEALLAKNKSL--NPQLaLKVGQVLQLPA 67
Cdd:COG1652   107 DAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANRDQikNPDL-IYPGQVLRIPA 161
PRK13914 PRK13914
invasion associated endopeptidase;
17-98 1.13e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 39.40  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  17 STAATVTVKPGDTLYGIARRQGVSLEALLAKNKSLNPQLAlkVGQVLQLPARSGTARV-----ATTMNggVVRPAGIRVS 91
Cdd:PRK13914   25 ASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIV--PGQKLQVNEVAAAEKTeksvsATWLN--VRSGAGVDNS 100


                  ....*..
gi 1906335194  92 AVLPVQG 98
Cdd:PRK13914  101 IITSIKG 107
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 21-65 1.32e-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: 38.88  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1906335194  21 TVTVKPGDTLYGIARRQGVS---LEALLAKNKSLNPQLALKVGQVLQL 65
Cdd:COG3061    71 EYTVQSGDTLSQIFRRLGLSasdLYALLAAEGDAKPLSRLKPGQELRF 118
FimV_core TIGR03505
FimV N-terminal domain; This region is found at, or about 200 amino acids from, the N-terminus ...
 28-76 5.85e-03

FimV N-terminal domain; This region is found at, or about 200 amino acids from, the N-terminus of FimV from Pseudomonas aeruginosa, TspA of Neisseria meningitidis, and related proteins. Disruption of FimV blocks twitching motility from type IV pili; Semmler, et al. suggest a role for this family in peptidoglycan layer remodelling required by type IV fimbrial systems. Most but not all members of this protein family have a C-terminal region recognized by TIGR03504. In between is a highly variable, often repeat-filled region rich in the negatively charged amino acids Asp and Glu.


Pssm-ID: 274615 [Multi-domain]  Cd Length: 74  Bit Score: 34.62  E-value: 5.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906335194  28 DTLYGIARR----QGVSLEALLAKNKSLNPQL-------ALKVGQVLQLPARSGTARVAT 76
Cdd:TIGR03505   1 DTLWGIAQRvrpdNSVSLYQMMLALYRANPDAfiggninRLKVGQILRIPSEEEIQAVSP 60
 
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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