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Conserved domains on  [gi|492341520|ref|WP_005815497|]
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M23 family metallopeptidase [Desulfitobacterium hafniense]

Protein Classification

murein hydrolase activator EnvC( domain architecture ID 11471818)

murein hydrolase activator EnvC contains a M23 family metallopeptidase domain, it activates murein hydrolases AmiA and AmiB and plays a crucial role in daughter cell separation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-163 1.44e-22

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: 92.13  E-value: 1.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520  45 FPSPIQGKPLRvageYYSEELEMTLFHSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKVEVDCGEDWSVIYGGLKNLR 124
Cdd:COG4942  255 LPWPVSGRVVR----RFGERDGGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLL 330

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 492341520 125 VKEGDWVEVDQAIGQIGYypdiFGNIEQTHLHYEVWHGD 163
Cdd:COG4942  331 VKVGQRVKAGQPIGTVGS----SGGQGGPTLYFELRKNG 365
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-163 1.44e-22

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: 92.13  E-value: 1.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520  45 FPSPIQGKPLRvageYYSEELEMTLFHSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKVEVDCGEDWSVIYGGLKNLR 124
Cdd:COG4942  255 LPWPVSGRVVR----RFGERDGGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLL 330

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 492341520 125 VKEGDWVEVDQAIGQIGYypdiFGNIEQTHLHYEVWHGD 163
Cdd:COG4942  331 VKVGQRVKAGQPIGTVGS----SGGQGGPTLYFELRKNG 365
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 71-159 3.66e-20

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: 79.56  E-value: 3.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520  71 HSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKVEVDCGEDWSVIYGGLKNLRVKEGDWVEVDQAIGQIGYYpdifGNI 150
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNT----GRS 76


                 ....*....
gi 492341520 151 EQTHLHYEV 159
Cdd:cd12797   77 TGPHLHFEI 85
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 70-163 8.24e-18

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: 73.73  E-value: 8.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520   70 FHSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKVEVDCGEDWSVIYGGLKNLRVKEGDWVEVDQAIGQIGYypdiFGN 149
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGS----TGR 77

                          90
                  ....*....|....
gi 492341520  150 IEQTHLHYEVWHGD 163
Cdd:pfam01551  78 STGPHLHFEIRKNG 91
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-163 1.44e-22

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: 92.13  E-value: 1.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520  45 FPSPIQGKPLRvageYYSEELEMTLFHSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKVEVDCGEDWSVIYGGLKNLR 124
Cdd:COG4942  255 LPWPVSGRVVR----RFGERDGGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLL 330

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 492341520 125 VKEGDWVEVDQAIGQIGYypdiFGNIEQTHLHYEVWHGD 163
Cdd:COG4942  331 VKVGQRVKAGQPIGTVGS----SGGQGGPTLYFELRKNG 365
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 70-168 1.13e-21

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: 86.57  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520  70 FHSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKVEVDCGEDWSVIYGGLKNLRVKEGDWVEVDQAIGQIGyypdIFGN 149
Cdd:COG0739   96 FHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVG----NTGR 171

                         90
                 ....*....|....*....
gi 492341520 150 IEQTHLHYEVWHGDlVQVD 168
Cdd:COG0739  172 STGPHLHFEVRVNG-KPVD 189
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 71-159 3.66e-20

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: 79.56  E-value: 3.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520  71 HSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKVEVDCGEDWSVIYGGLKNLRVKEGDWVEVDQAIGQIGYYpdifGNI 150
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNT----GRS 76


                 ....*....
gi 492341520 151 EQTHLHYEV 159
Cdd:cd12797   77 TGPHLHFEI 85
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 70-163 8.24e-18

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: 73.73  E-value: 8.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520   70 FHSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKVEVDCGEDWSVIYGGLKNLRVKEGDWVEVDQAIGQIGYypdiFGN 149
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGS----TGR 77

                          90
                  ....*....|....
gi 492341520  150 IEQTHLHYEVWHGD 163
Cdd:pfam01551  78 STGPHLHFEIRKNG 91
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 28-168 3.08e-16

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: 72.37  E-value: 3.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520  28 QEDPVTKSEPVVRTLEDFPSPIQGKPLRVAGEY--YSEELEMTLFHSGTDYAQAEGAVIRVKHAGRVTYAGPDPFLGHKV 105
Cdd:COG5821   52 ESNEKSKSKVTASTSNKFLKPVSGKITREFGEDlvYSKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITV 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492341520 106 EVDCGEDWSVIYGGL-KNLRVKEGDWVEVDQAIGQIGyYPDIFGNIEQTHLHYEVWHGDlVQVD 168
Cdd:COG5821  132 VIDHGNGIKTVYANLdSKIKVKVGQKVKKGQVIGKVG-STALFESSEGPHLHFEVLKNG-KPVD 193
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 18-163 6.04e-07

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 47.29  E-value: 6.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492341520  18 FGGS-ALLAEGQEDPVTKSEPvvrtlEDFPSPIQGKplrvageyYSEELEMTlfHSGTDYAQAEGAVIRVKHAGRVTYAG 96
Cdd:COG5833   81 FGGPlAFLPPFGKEEETVEQG-----EAFALPVSGK--------VVESFQEN--GKGVDIETPGGANVKAVKEGYVIFAG 145

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492341520  97 PDPFLGHKVEVDCGEDWSVIYGGLKNLRVKEGDWVEVDQAIGQIGYypdifGNIEQTHLHYEVWHGD 163
Cdd:COG5833  146 KDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPA-----TEGEEGTFYFAIKKGG 207
 
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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