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Conserved domains on  [gi|1094405351|emb|SEL12944|]
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Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Jannaschia helgolandensis]

Protein Classification

M23 family metallopeptidase( domain architecture ID 18340547)

M23 family metallopeptidase is an endopeptidase that lyses bacterial cell wall peptidoglycans; also contains uncharacterized N-terminal DUF5930 domain

EC:  3.4.-.-
MEROPS:  M23
PubMed:  10493853|7674922
SCOP:  4000931

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF5930 pfam19353
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. ...
37-361 1.20e-156

Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. This family of proteins is found in rhodobacteria. Proteins in this family are typically between 411 and 445 amino acids in length. The family is found to the N-terminus of pfam01551.


:

Pssm-ID: 466052 [Multi-domain]  Cd Length: 320  Bit Score: 446.93  E-value: 1.20e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  37 VKQRLSDKINAKLERHLPEQRLFLKSEEGTRFIRLRPLTQASTLIGGALVVGWTVVVTSFFLIGAITSGSSRDQTARAQI 116
Cdd:pfam19353   1 MRTRLAIRLHALLERYFPERRLFLRSDTDTRFIRLRPLTQLIALAGGALVVGWTIIATAILLMDSIGSGNFREQAKRDQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 117 AYETRLAALSTERDTRAQEAEQALERFYSALDEVSKMQGTVLTSEQRVRELETGIEVIQRTLRRTVSERNEARDEAESLL 196
Cdd:pfam19353  81 TYEQRLNALSAERDARAAEALAAQERFNAALEQVSVMQSELLASEERRRELETGIEVIQSTLRRTMKERDAARAELAALQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 197 ARLDNAPEATALAerlAADSAETAEILADALDATALARDEAMVVAMGADAEITRMEAMAEVVAERNNRIFSRLEDALETS 276
Cdd:pfam19353 161 AELEGGGAAAAAR---AADADATLDFLTAALAETAAERDQIAADAQDALAEADELALEIRLMEERNDQIFRQLEEAMTVS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 277 MVPLERVFNQAGISSDSLLQSVRSGYSGQGGPLEPVVVSTRGGAdlVDVDTARANRLMDKLEDVDMYRIAAESLPLGKPV 356
Cdd:pfam19353 238 VEPLDKMFRAAGLDPDRILDQVRRGYSGQGGPLTPLSFSTRGEE--PSPDEARANRILNQLDRLNLYRIAAEKAPFAMPV 315

                  ....*
gi 1094405351 357 KSAYR 361
Cdd:pfam19353 316 KSAFR 320
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
285-473 7.54e-58

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: 189.80  E-value: 7.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 285 NQAGISSDSLLQSVRSGYSGQGGPLEPVVVSTRGGADLVDVDTARANRLMDKLEDVDMYRIAAESLPLGKPVKSayRLTS 364
Cdd:COG0739     4 ALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKG--RITS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 365 AFGPR------WGRMHSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGE 438
Cdd:COG0739    82 GFGYRrhpvtgRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQ 161
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1094405351 439 TIGGMGDTGRVTGVHSHYEIRRNGEALNPNTFIKA 473
Cdd:COG0739   162 VIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA 196
 
Name Accession Description Interval E-value
DUF5930 pfam19353
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. ...
37-361 1.20e-156

Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. This family of proteins is found in rhodobacteria. Proteins in this family are typically between 411 and 445 amino acids in length. The family is found to the N-terminus of pfam01551.


Pssm-ID: 466052 [Multi-domain]  Cd Length: 320  Bit Score: 446.93  E-value: 1.20e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  37 VKQRLSDKINAKLERHLPEQRLFLKSEEGTRFIRLRPLTQASTLIGGALVVGWTVVVTSFFLIGAITSGSSRDQTARAQI 116
Cdd:pfam19353   1 MRTRLAIRLHALLERYFPERRLFLRSDTDTRFIRLRPLTQLIALAGGALVVGWTIIATAILLMDSIGSGNFREQAKRDQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 117 AYETRLAALSTERDTRAQEAEQALERFYSALDEVSKMQGTVLTSEQRVRELETGIEVIQRTLRRTVSERNEARDEAESLL 196
Cdd:pfam19353  81 TYEQRLNALSAERDARAAEALAAQERFNAALEQVSVMQSELLASEERRRELETGIEVIQSTLRRTMKERDAARAELAALQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 197 ARLDNAPEATALAerlAADSAETAEILADALDATALARDEAMVVAMGADAEITRMEAMAEVVAERNNRIFSRLEDALETS 276
Cdd:pfam19353 161 AELEGGGAAAAAR---AADADATLDFLTAALAETAAERDQIAADAQDALAEADELALEIRLMEERNDQIFRQLEEAMTVS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 277 MVPLERVFNQAGISSDSLLQSVRSGYSGQGGPLEPVVVSTRGGAdlVDVDTARANRLMDKLEDVDMYRIAAESLPLGKPV 356
Cdd:pfam19353 238 VEPLDKMFRAAGLDPDRILDQVRRGYSGQGGPLTPLSFSTRGEE--PSPDEARANRILNQLDRLNLYRIAAEKAPFAMPV 315

                  ....*
gi 1094405351 357 KSAYR 361
Cdd:pfam19353 316 KSAFR 320
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
285-473 7.54e-58

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: 189.80  E-value: 7.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 285 NQAGISSDSLLQSVRSGYSGQGGPLEPVVVSTRGGADLVDVDTARANRLMDKLEDVDMYRIAAESLPLGKPVKSayRLTS 364
Cdd:COG0739     4 ALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKG--RITS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 365 AFGPR------WGRMHSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGE 438
Cdd:COG0739    82 GFGYRrhpvtgRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQ 161
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1094405351 439 TIGGMGDTGRVTGVHSHYEIRRNGEALNPNTFIKA 473
Cdd:COG0739   162 VIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
372-467 6.52e-49

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: 162.72  E-value: 6.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 372 RMHSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGETIGGMGDTGRVTG 451
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80
                          90
                  ....*....|....*.
gi 1094405351 452 VHSHYEIRRNGEALNP 467
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
374-458 1.23e-40

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: 140.42  E-value: 1.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 374 HSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGETIGGMGDTGRVTGVH 453
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80

                  ....*
gi 1094405351 454 SHYEI 458
Cdd:cd12797    81 LHFEI 85
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
97-473 5.57e-40

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: 147.99  E-value: 5.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  97 FLIGAITSGSSRDQTARAQIAYETRLAALSTERDTRAQEAEQALERFYSALDEVSKMQGTVLTSEQRVRELETGIEVIQR 176
Cdd:COG4942     4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 177 TLRRTVSERNEARDEAESLLARLdnapeatalAERLAAdsaetaeiladalDATALARDEAMVVAMGADAE--ITRMEAM 254
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEEL---------AELLRA-------------LYRLGRQPPLALLLSPEDFLdaVRRLQYL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 255 AEVVAERNNRI---------FSRLEDALETSMVPLERVFNQAGISSDSLLQSVRSgysgQGGPLEPVVVSTRGGADLVDV 325
Cdd:COG4942   142 KYLAPARREQAeelradlaeLAALRAELEAERAELEALLAELEEERAALEALKAE----RQKLLARLEKELAELAAELAE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 326 DTARANRLMDKLEDVDMYRIAAESLPLGKPVKSAY---------RLTSAFGPR--WGRMHSGVDLAASRGTPILAAADGV 394
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKgklpwpvsgRVVRRFGERdgGGGRNKGIDIAAPPGAPVRAVADGT 297
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1094405351 395 VTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGETIGGMGDTGRVTGVHSHYEIRRNGEALNPNTFIKA 473
Cdd:COG4942   298 VVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAK 376
PRK11649 PRK11649
putative peptidase; Provisional
355-469 8.79e-26

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 109.37  E-value: 8.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 355 PVKSAYRLTSAFGPR-----WGRM--HSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIA 427
Cdd:PRK11649  287 PTAKQFRISSNFNPRrlnpvTGRVapHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLL 366
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1094405351 428 VTVGQRVSRGETIGGMGDTGRVTGVHSHYEIRRNGEALNPNT 469
Cdd:PRK11649  367 VKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLT 408
 
Name Accession Description Interval E-value
DUF5930 pfam19353
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. ...
37-361 1.20e-156

Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. This family of proteins is found in rhodobacteria. Proteins in this family are typically between 411 and 445 amino acids in length. The family is found to the N-terminus of pfam01551.


Pssm-ID: 466052 [Multi-domain]  Cd Length: 320  Bit Score: 446.93  E-value: 1.20e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  37 VKQRLSDKINAKLERHLPEQRLFLKSEEGTRFIRLRPLTQASTLIGGALVVGWTVVVTSFFLIGAITSGSSRDQTARAQI 116
Cdd:pfam19353   1 MRTRLAIRLHALLERYFPERRLFLRSDTDTRFIRLRPLTQLIALAGGALVVGWTIIATAILLMDSIGSGNFREQAKRDQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 117 AYETRLAALSTERDTRAQEAEQALERFYSALDEVSKMQGTVLTSEQRVRELETGIEVIQRTLRRTVSERNEARDEAESLL 196
Cdd:pfam19353  81 TYEQRLNALSAERDARAAEALAAQERFNAALEQVSVMQSELLASEERRRELETGIEVIQSTLRRTMKERDAARAELAALQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 197 ARLDNAPEATALAerlAADSAETAEILADALDATALARDEAMVVAMGADAEITRMEAMAEVVAERNNRIFSRLEDALETS 276
Cdd:pfam19353 161 AELEGGGAAAAAR---AADADATLDFLTAALAETAAERDQIAADAQDALAEADELALEIRLMEERNDQIFRQLEEAMTVS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 277 MVPLERVFNQAGISSDSLLQSVRSGYSGQGGPLEPVVVSTRGGAdlVDVDTARANRLMDKLEDVDMYRIAAESLPLGKPV 356
Cdd:pfam19353 238 VEPLDKMFRAAGLDPDRILDQVRRGYSGQGGPLTPLSFSTRGEE--PSPDEARANRILNQLDRLNLYRIAAEKAPFAMPV 315

                  ....*
gi 1094405351 357 KSAYR 361
Cdd:pfam19353 316 KSAFR 320
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
285-473 7.54e-58

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: 189.80  E-value: 7.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 285 NQAGISSDSLLQSVRSGYSGQGGPLEPVVVSTRGGADLVDVDTARANRLMDKLEDVDMYRIAAESLPLGKPVKSayRLTS 364
Cdd:COG0739     4 ALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKG--RITS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 365 AFGPR------WGRMHSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGE 438
Cdd:COG0739    82 GFGYRrhpvtgRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQ 161
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1094405351 439 TIGGMGDTGRVTGVHSHYEIRRNGEALNPNTFIKA 473
Cdd:COG0739   162 VIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
372-467 6.52e-49

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: 162.72  E-value: 6.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 372 RMHSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGETIGGMGDTGRVTG 451
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80
                          90
                  ....*....|....*.
gi 1094405351 452 VHSHYEIRRNGEALNP 467
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
374-458 1.23e-40

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: 140.42  E-value: 1.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 374 HSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGETIGGMGDTGRVTGVH 453
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80

                  ....*
gi 1094405351 454 SHYEI 458
Cdd:cd12797    81 LHFEI 85
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
97-473 5.57e-40

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: 147.99  E-value: 5.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  97 FLIGAITSGSSRDQTARAQIAYETRLAALSTERDTRAQEAEQALERFYSALDEVSKMQGTVLTSEQRVRELETGIEVIQR 176
Cdd:COG4942     4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 177 TLRRTVSERNEARDEAESLLARLdnapeatalAERLAAdsaetaeiladalDATALARDEAMVVAMGADAE--ITRMEAM 254
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEEL---------AELLRA-------------LYRLGRQPPLALLLSPEDFLdaVRRLQYL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 255 AEVVAERNNRI---------FSRLEDALETSMVPLERVFNQAGISSDSLLQSVRSgysgQGGPLEPVVVSTRGGADLVDV 325
Cdd:COG4942   142 KYLAPARREQAeelradlaeLAALRAELEAERAELEALLAELEEERAALEALKAE----RQKLLARLEKELAELAAELAE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 326 DTARANRLMDKLEDVDMYRIAAESLPLGKPVKSAY---------RLTSAFGPR--WGRMHSGVDLAASRGTPILAAADGV 394
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALKgklpwpvsgRVVRRFGERdgGGGRNKGIDIAAPPGAPVRAVADGT 297
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1094405351 395 VTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGETIGGMGDTGRVTGVHSHYEIRRNGEALNPNTFIKA 473
Cdd:COG4942   298 VVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAK 376
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
334-472 2.37e-38

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: 138.24  E-value: 2.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 334 MDKLEDVDMYRIAAESLPLGKPVKSayRLTSAFGPR---------WgRMHSGVDLAASRGTPILAAADGVVTFAGWSSAY 404
Cdd:COG5821    51 SESNEKSKSKVTASTSNKFLKPVSG--KITREFGEDlvysktlneW-RTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKY 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1094405351 405 GKLIKIRHPLGFETRYAH-NDSIAVTVGQRVSRGETIGGMGDTGRV---TGVHSHYEIRRNGEALNPNTFIK 472
Cdd:COG5821   128 GITVVIDHGNGIKTVYANlDSKIKVKVGQKVKKGQVIGKVGSTALFessEGPHLHFEVLKNGKPVDPMKYLK 199
PRK11649 PRK11649
putative peptidase; Provisional
355-469 8.79e-26

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 109.37  E-value: 8.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 355 PVKSAYRLTSAFGPR-----WGRM--HSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIA 427
Cdd:PRK11649  287 PTAKQFRISSNFNPRrlnpvTGRVapHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLL 366
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1094405351 428 VTVGQRVSRGETIGGMGDTGRVTGVHSHYEIRRNGEALNPNT 469
Cdd:PRK11649  367 VKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLT 408
nlpD PRK10871
murein hydrolase activator NlpD;
376-467 4.52e-18

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 84.89  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 376 GVDLAASRGTPILAAADGVVTFAGWS-SAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGETIGGMGDTGrVTGVHS 454
Cdd:PRK10871  221 GIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTG-TSSTRL 299
                          90
                  ....*....|...
gi 1094405351 455 HYEIRRNGEALNP 467
Cdd:PRK10871  300 HFEIRYKGKSVNP 312
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
374-472 2.68e-14

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 71.95  E-value: 2.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 374 HSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRYAHNDSIAVTVGQRVSRGETIggmgdtGRVTGVH 453
Cdd:COG5833   120 GKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKI------GTVPATE 193
                          90       100
                  ....*....|....*....|....
gi 1094405351 454 S-----HYEIRRNGEALNPNTFIK 472
Cdd:COG5833   194 GeegtfYFAIKKGGKFIDPIQVIS 217
PRK11637 PRK11637
AmiB activator; Provisional
352-467 2.14e-11

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 65.48  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 352 LGKPVKSAY-----RLTSAFGP------RWgrmhSGVDLAASRGTPILAAADGVVTFAGWSSAYGKLIKIRHPLGFETRY 420
Cdd:PRK11637  300 LGRPRGQAFwpvrgPTLHRFGEqlqgelRW----KGMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLY 375
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1094405351 421 AHNDSIAVTVGQRVSRGETIGGMGDTGRVTGVHSHYEIRRNGEALNP 467
Cdd:PRK11637  376 GYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNP 422
PRK06148 PRK06148
hypothetical protein; Provisional
364-458 1.26e-07

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 54.26  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  364 SAFGPRW---GR--MHSGVDLAASRGTPILAAADGVVTFAGWSSA---YGKLIKIRH--PLG--FETRYAHNDSIAV--- 428
Cdd:PRK06148   426 EAFTSRFiegERrtVHLGVDLFAPAGTPVYAPLAGTVRSVEIEAVplgYGGLVALEHetPGGdpFYTLYGHLAHEAVsrl 505
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1094405351  429 TVGQRVSRGETIGGMGDTGRVTG--VHSHYEI 458
Cdd:PRK06148   506 KPGDRLAAGELFGAMGDAHENGGwaPHLHFQL 537
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
108-274 3.91e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 108 RDQTARAQIAY-ETRLAALSTERDTRAQEAEQALERFYSALDEVSKMQGTVLTSEQRVRELETGIEVIQRTLRRTVSERN 186
Cdd:COG1196   240 ELEELEAELEElEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 187 EARDEAESLLARLDNAPEATALAERLAADSAETAEILADALDATALARDEAmvvamgadaeITRMEAMAEVVAERNNRIF 266
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA----------EAELAEAEEELEELAEELL 389

                  ....*...
gi 1094405351 267 SRLEDALE 274
Cdd:COG1196   390 EALRAAAE 397
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-215 2.77e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  108 RDQTARAQIAYETRLAALSTERDTRA-----QEAEQALERFYSALDEVSKMQGTVLTSEQRVRELETGIEVIQRTLRRTV 182
Cdd:COG4913    640 LDALQERREALQRLAEYSWDEIDVASaereiAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1094405351  183 SERNEARDEAESLLARLDNAPEATALAERLAAD 215
Cdd:COG4913    720 KELEQAEEELDELQDRLEAAEDLARLELRALLE 752
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
108-275 5.37e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 108 RDQTARAQIAYETRLAALSTERDTRAQEAEQALERFYSALDEVSKMQGTVLTSEQRVRELETGIEVIQRTLRRTVSERNE 187
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351 188 ARDEAESLLARLDNAPEATALAERLAADSAETAEILADALDATALARDEAmvvamgADAEITRMEAMAEVVAERNNRIFS 267
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE------EEALEEAAEEEAELEEEEEALLEL 464

                  ....*...
gi 1094405351 268 RLEDALET 275
Cdd:COG1196   465 LAELLEEA 472
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
112-274 8.24e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 8.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  112 ARAQIAYETRLAALSTERDTRAQEAEQALERFYSALDEVSKMQGTVLTSE-QRVRELETGIEviqrTLRRTVSERNEARD 190
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIE----RLERELEERERRRA 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1094405351  191 EAESLLARLDNAPEATALA-ERLAADSAETAEILADALDATALARDEAMVVAMGADAEITRMEAMAEVVAERNNRIFSRL 269
Cdd:COG4913    363 RLEALLAALGLPLPASAEEfAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442

                   ....*
gi 1094405351  270 EDALE 274
Cdd:COG4913    443 LALRD 447
 
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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