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Conserved domains on  [gi|1871972454|ref|WP_179993073|]
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MULTISPECIES: M23 family metallopeptidase [Acinetobacter]

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 ...
 56-182 2.18e-34

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: 120.08  E-value: 2.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  56 PVQGvkprQIQDTWGGARS----EGRKHEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDY 131
Cdd:COG0739    74 PVKG----RITSGFGYRRHpvtgRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSI 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1871972454 132 AehIQEGDWVEAGEIIAYVGNTGNAknTPPHLHYGIYLSGEgATNPYPYLK 182
Cdd:COG0739   150 L--VKVGQRVKAGQVIGYVGNTGRS--TGPHLHFEVRVNGK-PVDPLPFLP 195
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 56-182 2.18e-34

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: 120.08  E-value: 2.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  56 PVQGvkprQIQDTWGGARS----EGRKHEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDY 131
Cdd:COG0739    74 PVKG----RITSGFGYRRHpvtgRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSI 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1871972454 132 AehIQEGDWVEAGEIIAYVGNTGNAknTPPHLHYGIYLSGEgATNPYPYLK 182
Cdd:COG0739   150 L--VKVGQRVKAGQVIGYVGNTGRS--TGPHLHFEVRVNGK-PVDPLPFLP 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 77-177 8.69e-28

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: 99.93  E-value: 8.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  77 RKHEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDYAehIQEGDWVEAGEIIAYVGNTGNA 156
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSIL--VKVGQRVKAGQVIGTVGSTGRS 78

                          90       100
                  ....*....|....*....|.
gi 1871972454 157 knTPPHLHYGIYLSGEgATNP 177
Cdd:pfam01551  79 --TGPHLHFEIRKNGK-PVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 79-167 1.28e-26

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: 96.89  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  79 HEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDYaeHIQEGDWVEAGEIIAYVGNTGNAkn 158
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSI--LVKVGQRVKKGQVIGTVGNTGRS-- 76


                  ....*....
gi 1871972454 159 TPPHLHYGI 167
Cdd:cd12797    77 TGPHLHFEI 85
PRK06148 PRK06148
hypothetical protein; Provisional
 79-173 6.01e-06

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 45.79  E-value: 6.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454   79 HEGTDIFAQRGTPVVSATQGIVR--KIGTNNLG-GKVIWI--TGPNLSQHY--YAHLE-DYAEHIQEGDWVEAGEIIAYV 150
Cdd:PRK06148   441 HLGVDLFAPAGTPVYAPLAGTVRsvEIEAVPLGyGGLVALehETPGGDPFYtlYGHLAhEAVSRLKPGDRLAAGELFGAM 520

                           90       100
                   ....*....|....*....|...
gi 1871972454  151 GNTGNAKNTPPHLHYGIYLSGEG 173
Cdd:PRK06148   521 GDAHENGGWAPHLHFQLSTDTSL 543
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 56-182 2.18e-34

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: 120.08  E-value: 2.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  56 PVQGvkprQIQDTWGGARS----EGRKHEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDY 131
Cdd:COG0739    74 PVKG----RITSGFGYRRHpvtgRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSI 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1871972454 132 AehIQEGDWVEAGEIIAYVGNTGNAknTPPHLHYGIYLSGEgATNPYPYLK 182
Cdd:COG0739   150 L--VKVGQRVKAGQVIGYVGNTGRS--TGPHLHFEVRVNGK-PVDPLPFLP 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 77-177 8.69e-28

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: 99.93  E-value: 8.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  77 RKHEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDYAehIQEGDWVEAGEIIAYVGNTGNA 156
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSIL--VKVGQRVKAGQVIGTVGSTGRS 78

                          90       100
                  ....*....|....*....|.
gi 1871972454 157 knTPPHLHYGIYLSGEgATNP 177
Cdd:pfam01551  79 --TGPHLHFEIRKNGK-PVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 79-167 1.28e-26

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: 96.89  E-value: 1.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  79 HEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDYaeHIQEGDWVEAGEIIAYVGNTGNAkn 158
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSI--LVKVGQRVKKGQVIGTVGNTGRS-- 76


                  ....*....
gi 1871972454 159 TPPHLHYGI 167
Cdd:cd12797    77 TGPHLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 77-182 6.54e-22

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: 87.77  E-value: 6.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  77 RKHEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDYAEhIQEGDWVEAGEIIAYVGNTG-N 155
Cdd:COG5821    95 RTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANLDSKIK-VKVGQKVKKGQVIGKVGSTAlF 173

                          90       100
                  ....*....|....*....|....*..
gi 1871972454 156 AKNTPPHLHYGIYLSGEgATNPYPYLK 182
Cdd:COG5821   174 ESSEGPHLHFEVLKNGK-PVDPMKYLK 199
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 56-182 1.69e-21

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: 89.82  E-value: 1.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  56 PVQGvkprQIQDTWGGARSEGRKHEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWItgpNLSQHY---YAHLEDYa 132
Cdd:COG4942   258 PVSG----RVVRRFGERDGGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVII---DHGGGYltlYAHLSSL- 329

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1871972454 133 eHIQEGDWVEAGEIIAYVGNTGNakNTPPHLHYGIYLSGEgATNPYPYLK 182
Cdd:COG4942   330 -LVKVGQRVKAGQPIGTVGSSGG--QGGPTLYFELRKNGK-PVDPLPWLA 375
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 79-168 2.36e-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: 48.83  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  79 HEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDYAehIQEGDWVEAGEIIayvGNTGNAKN 158
Cdd:COG5833   120 GKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSID--VKLYDFVEAGQKI---GTVPATEG 194

                          90
                  ....*....|
gi 1871972454 159 TPPHLHYGIY 168
Cdd:COG5833   195 EEGTFYFAIK 204
PRK06148 PRK06148
hypothetical protein; Provisional
 79-173 6.01e-06

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 45.79  E-value: 6.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454   79 HEGTDIFAQRGTPVVSATQGIVR--KIGTNNLG-GKVIWI--TGPNLSQHY--YAHLE-DYAEHIQEGDWVEAGEIIAYV 150
Cdd:PRK06148   441 HLGVDLFAPAGTPVYAPLAGTVRsvEIEAVPLGyGGLVALehETPGGDPFYtlYGHLAhEAVSRLKPGDRLAAGELFGAM 520

                           90       100
                   ....*....|....*....|...
gi 1871972454  151 GNTGNAKNTPPHLHYGIYLSGEG 173
Cdd:PRK06148   521 GDAHENGGWAPHLHFQLSTDTSL 543
PRK11649 PRK11649
putative peptidase; Provisional
 79-177 4.07e-04

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 40.03  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972454  79 HEGTDIFAQRGTPVVSATQGIVRKIGTNNLGGKVIWITGPNLSQHYYAHLEDYAehIQEGDWVEAGEIIAYVGNTGnaKN 158
Cdd:PRK11649  313 HRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLL--VKPGQKVKRGDRIALSGNTG--RS 388

                          90
                  ....*....|....*....
gi 1871972454 159 TPPHLHYGIYLSGEgATNP 177
Cdd:PRK11649  389 TGPHLHYEVWINQQ-AVNP 406
 
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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