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Conserved domains on  [gi|1233017184|gb|ASU32614.1|]
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peptidase M23 [Mucilaginibacter xinganensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06148 super family cl32120
hypothetical protein; Provisional
 2-229 6.91e-45

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK06148:

Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 160.19  E-value: 6.91e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184    2 DAAARLAAYFKTHPANIGKVVDFDAGAHRLYHFDFTAANHDLDAdtFSDTVKFSRWVNKKLSEHDCKYGVGGYLEHRTIY 81
Cdd:PRK06148   346 EGAGRVRAWLDANRGAFAPLVGPDLATLPKASVPVGDAAHPDSA--GQRPAEAAAWWDEFCARTGAQLGIGPYGEPRLVY 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184   82 ARSAhFD---TDDEPRRLHLGVDIWANVGTLVYSPLDGIVHSYQDNNNFGDYGPTIILQHQLDDLT-LYTLYGHLSRESL 157
Cdd:PRK06148   424 TDEA-FTsrfIEGERRTVHLGVDLFAPAGTPVYAPLAGTVRSVEIEAVPLGYGGLVALEHETPGGDpFYTLYGHLAHEAV 502

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233017184  158 DGLYVGKSVSKNERIATFGVIEENGHWPPHLHFQLIFDMQGKLGDYPGVCRYSEKERYQQNIPDPQLILKFP 229
Cdd:PRK06148   503 SRLKPGDRLAAGELFGAMGDAHENGGWAPHLHFQLSTDTSLSATEWPGVGEPDYLDVWAALFPDPAALLGLP 574
 
Name Accession Description Interval E-value
PRK06148 PRK06148
hypothetical protein; Provisional
 2-229 6.91e-45

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 160.19  E-value: 6.91e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184    2 DAAARLAAYFKTHPANIGKVVDFDAGAHRLYHFDFTAANHDLDAdtFSDTVKFSRWVNKKLSEHDCKYGVGGYLEHRTIY 81
Cdd:PRK06148   346 EGAGRVRAWLDANRGAFAPLVGPDLATLPKASVPVGDAAHPDSA--GQRPAEAAAWWDEFCARTGAQLGIGPYGEPRLVY 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184   82 ARSAhFD---TDDEPRRLHLGVDIWANVGTLVYSPLDGIVHSYQDNNNFGDYGPTIILQHQLDDLT-LYTLYGHLSRESL 157
Cdd:PRK06148   424 TDEA-FTsrfIEGERRTVHLGVDLFAPAGTPVYAPLAGTVRSVEIEAVPLGYGGLVALEHETPGGDpFYTLYGHLAHEAV 502

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233017184  158 DGLYVGKSVSKNERIATFGVIEENGHWPPHLHFQLIFDMQGKLGDYPGVCRYSEKERYQQNIPDPQLILKFP 229
Cdd:PRK06148   503 SRLKPGDRLAAGELFGAMGDAHENGGWAPHLHFQLSTDTSLSATEWPGVGEPDYLDVWAALFPDPAALLGLP 574
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 94-195 6.68e-20

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: 83.87  E-value: 6.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  94 RRLHLGVDIWANVGTLVYSPLDGIVHSYQDNnnfGDYGPTIILQHqldDLTLYTLYGHLSRESldgLYVGKSVSKNERIA 173
Cdd:COG0739    94 RRFHKGIDIAAPTGTPVYAAADGTVVFAGWN---GGYGNLVIIDH---GNGYTTLYAHLSSIL---VKVGQRVKAGQVIG 164

                          90       100
                  ....*....|....*....|....
gi 1233017184 174 TFGvieeNGHWP--PHLHFQLIFD 195
Cdd:COG0739   165 YVG----NTGRStgPHLHFEVRVN 184
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 95-192 4.14e-15

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: 68.34  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  95 RLHLGVDIWANVGTLVYSPLDGIVhSYQDNNNFgdYGPTIILQHqldDLTLYTLYGHLSRESLDglyVGKSVSKNERIAT 174
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVV-VFAGWLGG--YGNLVIIDH---GNGYSTLYAHLSSILVK---VGQRVKAGQVIGT 71

                          90
                  ....*....|....*...
gi 1233017184 175 FGVIEENGhwPPHLHFQL 192
Cdd:pfam01551  72 VGSTGRST--GPHLHFEI 87
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 97-192 6.85e-14

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: 64.92  E-value: 6.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  97 HLGVDIWANVGTLVYSPLDGIVHSYQDNnnfGDYGPTIILQHqldDLTLYTLYGHLSRESLDglyVGKSVSKNERIATFG 176
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD---GGYGNYVIIDH---GNGYYTLYAHLSSILVK---VGQRVKKGQVIGTVG 71

                          90
                  ....*....|....*.
gi 1233017184 177 viEENGHWPPHLHFQL 192
Cdd:cd12797    72 --NTGRSTGPHLHFEI 85
 
Name Accession Description Interval E-value
PRK06148 PRK06148
hypothetical protein; Provisional
 2-229 6.91e-45

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 160.19  E-value: 6.91e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184    2 DAAARLAAYFKTHPANIGKVVDFDAGAHRLYHFDFTAANHDLDAdtFSDTVKFSRWVNKKLSEHDCKYGVGGYLEHRTIY 81
Cdd:PRK06148   346 EGAGRVRAWLDANRGAFAPLVGPDLATLPKASVPVGDAAHPDSA--GQRPAEAAAWWDEFCARTGAQLGIGPYGEPRLVY 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184   82 ARSAhFD---TDDEPRRLHLGVDIWANVGTLVYSPLDGIVHSYQDNNNFGDYGPTIILQHQLDDLT-LYTLYGHLSRESL 157
Cdd:PRK06148   424 TDEA-FTsrfIEGERRTVHLGVDLFAPAGTPVYAPLAGTVRSVEIEAVPLGYGGLVALEHETPGGDpFYTLYGHLAHEAV 502

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1233017184  158 DGLYVGKSVSKNERIATFGVIEENGHWPPHLHFQLIFDMQGKLGDYPGVCRYSEKERYQQNIPDPQLILKFP 229
Cdd:PRK06148   503 SRLKPGDRLAAGELFGAMGDAHENGGWAPHLHFQLSTDTSLSATEWPGVGEPDYLDVWAALFPDPAALLGLP 574
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 94-195 6.68e-20

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: 83.87  E-value: 6.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  94 RRLHLGVDIWANVGTLVYSPLDGIVHSYQDNnnfGDYGPTIILQHqldDLTLYTLYGHLSRESldgLYVGKSVSKNERIA 173
Cdd:COG0739    94 RRFHKGIDIAAPTGTPVYAAADGTVVFAGWN---GGYGNLVIIDH---GNGYTTLYAHLSSIL---VKVGQRVKAGQVIG 164

                          90       100
                  ....*....|....*....|....
gi 1233017184 174 TFGvieeNGHWP--PHLHFQLIFD 195
Cdd:COG0739   165 YVG----NTGRStgPHLHFEVRVN 184
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 84-192 4.95e-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: 75.96  E-value: 4.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  84 SAHFDTDDEPRRLHLGVDIWANVGTLVYSPLDGIVhSYQDnnNFGDYGPTIILQHQlDDltLYTLYGHLSResldgLYV- 162
Cdd:COG4942   264 VRRFGERDGGGGRNKGIDIAAPPGAPVRAVADGTV-VYAG--WLRGYGNLVIIDHG-GG--YLTLYAHLSS-----LLVk 332

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1233017184 163 -GKSVSKNERIATFGVIEENGhwPPHLHFQL 192
Cdd:COG4942   333 vGQRVKAGQPIGTVGSSGGQG--GPTLYFEL 361
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 95-192 4.14e-15

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: 68.34  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  95 RLHLGVDIWANVGTLVYSPLDGIVhSYQDNNNFgdYGPTIILQHqldDLTLYTLYGHLSRESLDglyVGKSVSKNERIAT 174
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVV-VFAGWLGG--YGNLVIIDH---GNGYSTLYAHLSSILVK---VGQRVKAGQVIGT 71

                          90
                  ....*....|....*...
gi 1233017184 175 FGVIEENGhwPPHLHFQL 192
Cdd:pfam01551  72 VGSTGRST--GPHLHFEI 87
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 97-192 6.85e-14

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: 64.92  E-value: 6.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  97 HLGVDIWANVGTLVYSPLDGIVHSYQDNnnfGDYGPTIILQHqldDLTLYTLYGHLSRESLDglyVGKSVSKNERIATFG 176
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD---GGYGNYVIIDH---GNGYYTLYAHLSSILVK---VGQRVKKGQVIGTVG 71

                          90
                  ....*....|....*.
gi 1233017184 177 viEENGHWPPHLHFQL 192
Cdd:cd12797    72 --NTGRSTGPHLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 95-192 3.25e-11

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: 60.43  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  95 RLHLGVDIWANVGTLVYSPLDGIVHSYQDNnnfGDYGPTIILQHQlDDLTlyTLYGHLSRESLdgLYVGKSVSKNERIAT 174
Cdd:COG5821    95 RTHTGIDIAAKEGTPVKAAADGVVVEVGKD---PKYGITVVIDHG-NGIK--TVYANLDSKIK--VKVGQKVKKGQVIGK 166

                          90       100
                  ....*....|....*....|.
gi 1233017184 175 FG---VIEENGhwPPHLHFQL 192
Cdd:COG5821   167 VGstaLFESSE--GPHLHFEV 185
PRK06149 PRK06149
aminotransferase;
85-229 2.25e-05

aminotransferase;


Pssm-ID: 235716 [Multi-domain]  Cd Length: 972  Bit Score: 44.99  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  85 AHFDTDDEPRRLHLGVDIWANVGTLVYSPLDGIVHSyqdnnnfgDYGPTIILQHQLDDLTLYTLYGHLSresldglyVGK 164
Cdd:PRK06149  420 TPLLSAREPATFALGVDLCLPAGTAVAAPFAGTVVR--------DGQGHLTLRGDALELHLDGVEPAVE--------DGA 483

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1233017184 165 SVSKNERIATFGvieenGHWPPHLHFQLIFDMQGklgdyPGVCRYSEKERYQQNIPDPQLILKFP 229
Cdd:PRK06149  484 AVRAGDPLGSVA-----GEGPLRVQLCPVAGLVP-----PLFARPSQAAAWLALCPSPAPLLGLP 538
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 99-192 3.75e-03

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 37.28  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233017184  99 GVDIWANVGTLVYSPLDGIVhSYQDNNNfgDYGPTIILQHQlDDltLYTLYGHLSRESLDglyVGKSVSKNERIATFGVI 178
Cdd:COG5833   122 GVDIETPGGANVKAVKEGYV-IFAGKDE--ETGKTVIIQHA-DG--SESWYGNLSSIDVK---LYDFVEAGQKIGTVPAT 192

                          90
                  ....*....|....
gi 1233017184 179 EENghwPPHLHFQL 192
Cdd:COG5833   193 EGE---EGTFYFAI 203
 
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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