NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|818370573|gb|KKQ50778|]
View 

Peptidase M23 [Candidatus Woesebacteria bacterium GW2011_GWD1_38_10]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 123-269 8.45e-24

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: 97.35  E-value: 8.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 123 RMTASFdhnklGNRFQPFTTetyikkdcpngvygitCYDSHNGTDFSANKiqGDyDVLPVADGEVVYVSDTSksgkcmis 202
Cdd:COG0739   78 RITSGF-----GYRRHPVTG----------------RRRFHKGIDIAAPT--GT-PVYAAADGTVVFAGWNG-------- 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818370573 203 knSYGCVVIIKHSaNNLYTLYAHLSEIYTKAGDNVKYTDIIGKMGNTGC--GPkcgvHLHLGTLIDKTP 269
Cdd:COG0739  126 --GYGNLVIIDHG-NGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRstGP----HLHFEVRVNGKP 187
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 123-269 8.45e-24

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: 97.35  E-value: 8.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 123 RMTASFdhnklGNRFQPFTTetyikkdcpngvygitCYDSHNGTDFSANKiqGDyDVLPVADGEVVYVSDTSksgkcmis 202
Cdd:COG0739   78 RITSGF-----GYRRHPVTG----------------RRRFHKGIDIAAPT--GT-PVYAAADGTVVFAGWNG-------- 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818370573 203 knSYGCVVIIKHSaNNLYTLYAHLSEIYTKAGDNVKYTDIIGKMGNTGC--GPkcgvHLHLGTLIDKTP 269
Cdd:COG0739  126 --GYGNLVIIDHG-NGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRstGP----HLHFEVRVNGKP 187
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 163-262 4.23e-23

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: 91.88  E-value: 4.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 163 HNGTDFSANKiqgDYDVLPVADGEVVYVSDtsksgkcmisKNSYGCVVIIKHsANNLYTLYAHLSEIYTKAGDNVKYTDI 242
Cdd:cd12797    1 HNGIDIAAPE---GTPVYAAADGTVVFAGW----------DGGYGNYVIIDH-GNGYYTLYAHLSSILVKVGQRVKKGQV 66

                         90       100
                 ....*....|....*....|
gi 818370573 243 IGKMGNTGCGPkcGVHLHLG 262
Cdd:cd12797   67 IGTVGNTGRST--GPHLHFE 84
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 163-269 1.95e-22

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: 90.30  E-value: 1.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573  163 HNGTDFSANKiqGDyDVLPVADGEVVYVSDTSksgkcmisknSYGCVVIIKHsANNLYTLYAHLSEIYTKAGDNVKYTDI 242
Cdd:pfam01551   3 HKGIDIAAPT--GT-PVYAAADGVVVFAGWLG----------GYGNLVIIDH-GNGYSTLYAHLSSILVKVGQRVKAGQV 68

                          90       100
                  ....*....|....*....|....*..
gi 818370573  243 IGKMGNTGCGPkcGVHLHLGTLIDKTP 269
Cdd:pfam01551  69 IGTVGSTGRST--GPHLHFEIRKNGKP 93
PRK11649 PRK11649
putative peptidase; Provisional
 163-260 7.57e-07

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 50.82  E-value: 7.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 163 HNGTDFSANkiQGDyDVLPVADGEVVyvsdtsksgkcmISKNS--YGCVVIIKHsANNLYTLYAHLSEIYTKAGDNVKYT 240
Cdd:PRK11649 313 HRGVDFAMP--VGT-PVLAVGDGEVV------------VAKRSgaAGNYVAIRH-GRQYTTRYMHLRKLLVKPGQKVKRG 376

                         90       100
                 ....*....|....*....|..
gi 818370573 241 DIIGKMGNTG--CGPkcgvHLH 260
Cdd:PRK11649 377 DRIALSGNTGrsTGP----HLH 394
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 123-269 8.45e-24

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: 97.35  E-value: 8.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 123 RMTASFdhnklGNRFQPFTTetyikkdcpngvygitCYDSHNGTDFSANKiqGDyDVLPVADGEVVYVSDTSksgkcmis 202
Cdd:COG0739   78 RITSGF-----GYRRHPVTG----------------RRRFHKGIDIAAPT--GT-PVYAAADGTVVFAGWNG-------- 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818370573 203 knSYGCVVIIKHSaNNLYTLYAHLSEIYTKAGDNVKYTDIIGKMGNTGC--GPkcgvHLHLGTLIDKTP 269
Cdd:COG0739  126 --GYGNLVIIDHG-NGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRstGP----HLHFEVRVNGKP 187
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 163-262 4.23e-23

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: 91.88  E-value: 4.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 163 HNGTDFSANKiqgDYDVLPVADGEVVYVSDtsksgkcmisKNSYGCVVIIKHsANNLYTLYAHLSEIYTKAGDNVKYTDI 242
Cdd:cd12797    1 HNGIDIAAPE---GTPVYAAADGTVVFAGW----------DGGYGNYVIIDH-GNGYYTLYAHLSSILVKVGQRVKKGQV 66

                         90       100
                 ....*....|....*....|
gi 818370573 243 IGKMGNTGCGPkcGVHLHLG 262
Cdd:cd12797   67 IGTVGNTGRST--GPHLHFE 84
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 163-269 1.95e-22

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: 90.30  E-value: 1.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573  163 HNGTDFSANKiqGDyDVLPVADGEVVYVSDTSksgkcmisknSYGCVVIIKHsANNLYTLYAHLSEIYTKAGDNVKYTDI 242
Cdd:pfam01551   3 HKGIDIAAPT--GT-PVYAAADGVVVFAGWLG----------GYGNLVIIDH-GNGYSTLYAHLSSILVKVGQRVKAGQV 68

                          90       100
                  ....*....|....*....|....*..
gi 818370573  243 IGKMGNTGCGPkcGVHLHLGTLIDKTP 269
Cdd:pfam01551  69 IGTVGSTGRST--GPHLHFEIRKNGKP 93
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 160-269 6.24e-17

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: 78.14  E-value: 6.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 160 YDSHNGTDFSANKiqGDyDVLPVADGEVVYVSDTSKsgkcmisknsYGCVVIIKHSaNNLYTLYAHL-SEIYTKAGDNVK 238
Cdd:COG5821   94 WRTHTGIDIAAKE--GT-PVKAAADGVVVEVGKDPK----------YGITVVIDHG-NGIKTVYANLdSKIKVKVGQKVK 159

                         90       100       110
                 ....*....|....*....|....*....|..
gi 818370573 239 YTDIIGKMGNTG-CGPKCGVHLHLGTLIDKTP 269
Cdd:COG5821  160 KGQVIGKVGSTAlFESSEGPHLHFEVLKNGKP 191
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 163-258 7.75e-16

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: 77.88  E-value: 7.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 163 HNGTDFSANKiqGDyDVLPVADGEVVYVSDTSksgkcmisknSYGCVVIIKHSaNNLYTLYAHLSEIYTKAGDNVKYTDI 242
Cdd:COG4942  277 NKGIDIAAPP--GA-PVRAVADGTVVYAGWLR----------GYGNLVIIDHG-GGYLTLYAHLSSLLVKVGQRVKAGQP 342

                         90
                 ....*....|....*.
gi 818370573 243 IGKMGNTGCGPKCGVH 258
Cdd:COG4942  343 IGTVGSSGGQGGPTLY 358
PRK11649 PRK11649
putative peptidase; Provisional
 163-260 7.57e-07

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 50.82  E-value: 7.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370573 163 HNGTDFSANkiQGDyDVLPVADGEVVyvsdtsksgkcmISKNS--YGCVVIIKHsANNLYTLYAHLSEIYTKAGDNVKYT 240
Cdd:PRK11649 313 HRGVDFAMP--VGT-PVLAVGDGEVV------------VAKRSgaAGNYVAIRH-GRQYTTRYMHLRKLLVKPGQKVKRG 376

                         90       100
                 ....*....|....*....|..
gi 818370573 241 DIIGKMGNTG--CGPkcgvHLH 260
Cdd:PRK11649 377 DRIALSGNTGrsTGP----HLH 394
PRK06148 PRK06148
hypothetical protein; Provisional
 205-266 4.99e-04

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 42.32  E-value: 4.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818370573  205 SYGCVVIIKHSANN---LYTLYAHLSEIYT---KAGDNVKYTDIIGKMG----NTGCGPkcgvHLHLGTLID 266
Cdd:PRK06148  473 GYGGLVALEHETPGgdpFYTLYGHLAHEAVsrlKPGDRLAAGELFGAMGdaheNGGWAP----HLHFQLSTD 540
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH