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Conserved domains on  [gi|696361913|ref|WP_032937061|]
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MULTISPECIES: C40 family peptidase [Citrobacter]

Protein Classification

C40 family peptidase( domain architecture ID 11434971)

C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides; contains a Cys-His-His catalytic triad

CATH:  3.90.1720.10
EC:  3.4.-.-
Gene Ontology:  GO:0008233|GO:0006508|GO:0016787|GO:0008234|GO:0000270
MEROPS:  C40
PubMed:  12620121|11517925

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
124-246 1.90e-43

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 146.38  E-value: 1.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913 124 EVAIHRLEQQLGKPYLWGGTDPDeGFDCSGLIFYAYNKiLAAKLPRTANEMYHYRRAtiVANRDLRRGDLVFFHIHSRDI 203
Cdd:COG0791  101 EAIVAAALSYLGTPYVWGGTSPS-GFDCSGLVQYVYRQ-AGISLPRTSADQAAAGTP--VSRSELQPGDLVFFRTGGGGI 176

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 696361913 204 aDHMGVYLGQGQFIESPRTGETIRVSNLSDDFWQDHYLGARRI 246
Cdd:COG0791  177 -SHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSRYVGARRV 218
 
Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
124-246 1.90e-43

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 146.38  E-value: 1.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913 124 EVAIHRLEQQLGKPYLWGGTDPDeGFDCSGLIFYAYNKiLAAKLPRTANEMYHYRRAtiVANRDLRRGDLVFFHIHSRDI 203
Cdd:COG0791  101 EAIVAAALSYLGTPYVWGGTSPS-GFDCSGLVQYVYRQ-AGISLPRTSADQAAAGTP--VSRSELQPGDLVFFRTGGGGI 176

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 696361913 204 aDHMGVYLGQGQFIESPRTGETIRVSNLSDDFWQDHYLGARRI 246
Cdd:COG0791  177 -SHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSRYVGARRV 218
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 135-245 2.92e-40

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 134.33  E-value: 2.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913  135 GKPYLWGGTDPDeGFDCSGLIFYAYNKIlAAKLPRTANEMYHYRRATIVANrDLRRGDLVFFHIHSRdiADHMGVYLGQG 214
Cdd:pfam00877   1 GVPYRWGGGSPS-GFDCSGLVRYAFAKV-GIELPRSSGQQYNAGKKTIPKS-EPQRGDLVFFGTGKG--ISHVGIYLGNG 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 696361913  215 QFIESPrTGETIRVSNLSDDFWQDHYLGARR 245
Cdd:pfam00877  76 QMLHAS-TGGGVSISSLNGGYWQKRLVGVRR 105
PRK13914 PRK13914
invasion associated endopeptidase;
115-246 2.34e-16

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 77.92  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913 115 SSNHLHNITEVA-IHRLEQQLGKPYLWGGTDPDEgFDCSGLIFYAYNKIlAAKLPRTANEmyHYRRATIVANRDLRRGDL 193
Cdd:PRK13914 357 SSNNNSNSSASAiIAEAQKHLGKAYSWGGNGPTT-FDCSGYTKYVFAKA-GISLPRTSGA--QYASTTRISESQAKPGDL 432

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 696361913 194 VFFHIHSrDIAdHMGVYLGQGQFIESPRTGetIRVSNLSDDFWQDHYLGARRI 246
Cdd:PRK13914 433 VFFDYGS-GIS-HVGIYVGNGQMINAQDNG--VKYDNIHGSGWGKYLVGFGRV 481
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
 161-229 5.43e-03

P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+); Escherichia coli ZntA mediates resistance to toxic levels of selected divalent metal ions. ZntA has the highest selectivity for Pb(2+), followed by Zn(2+) and Cd(2+); it also shows low levels of activity with Cu(2+), Ni(2+), and Co(2+). It is upregulated by the transcription factor ZntR at high zinc concentrations. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319846 [Multi-domain]  Cd Length: 597  Bit Score: 37.77  E-value: 5.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913 161 KILAAKLPRTANEMYHYRRATIVANRdLRRGDLVFFHIHSRDIADhmGVYL-GQGQFIESPRTGETIRVS 229
Cdd:cd07546   91 KALMALVPETALREENGERREVPADS-LRPGDVIEVAPGGRLPAD--GELLsGFASFDESALTGESIPVE 157
 
Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
124-246 1.90e-43

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 146.38  E-value: 1.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913 124 EVAIHRLEQQLGKPYLWGGTDPDeGFDCSGLIFYAYNKiLAAKLPRTANEMYHYRRAtiVANRDLRRGDLVFFHIHSRDI 203
Cdd:COG0791  101 EAIVAAALSYLGTPYVWGGTSPS-GFDCSGLVQYVYRQ-AGISLPRTSADQAAAGTP--VSRSELQPGDLVFFRTGGGGI 176

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 696361913 204 aDHMGVYLGQGQFIESPRTGETIRVSNLSDDFWQDHYLGARRI 246
Cdd:COG0791  177 -SHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSRYVGARRV 218
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 135-245 2.92e-40

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 134.33  E-value: 2.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913  135 GKPYLWGGTDPDeGFDCSGLIFYAYNKIlAAKLPRTANEMYHYRRATIVANrDLRRGDLVFFHIHSRdiADHMGVYLGQG 214
Cdd:pfam00877   1 GVPYRWGGGSPS-GFDCSGLVRYAFAKV-GIELPRSSGQQYNAGKKTIPKS-EPQRGDLVFFGTGKG--ISHVGIYLGNG 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 696361913  215 QFIESPrTGETIRVSNLSDDFWQDHYLGARR 245
Cdd:pfam00877  76 QMLHAS-TGGGVSISSLNGGYWQKRLVGVRR 105
PRK13914 PRK13914
invasion associated endopeptidase;
115-246 2.34e-16

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 77.92  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913 115 SSNHLHNITEVA-IHRLEQQLGKPYLWGGTDPDEgFDCSGLIFYAYNKIlAAKLPRTANEmyHYRRATIVANRDLRRGDL 193
Cdd:PRK13914 357 SSNNNSNSSASAiIAEAQKHLGKAYSWGGNGPTT-FDCSGYTKYVFAKA-GISLPRTSGA--QYASTTRISESQAKPGDL 432

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 696361913 194 VFFHIHSrDIAdHMGVYLGQGQFIESPRTGetIRVSNLSDDFWQDHYLGARRI 246
Cdd:PRK13914 433 VFFDYGS-GIS-HVGIYVGNGQMINAQDNG--VKYDNIHGSGWGKYLVGFGRV 481
spr PRK10838
bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;
135-251 8.08e-15

bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;


Pssm-ID: 236773 [Multi-domain]  Cd Length: 190  Bit Score: 70.56  E-value: 8.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913 135 GKPYLWGGtDPDEGFDCSGLIFYAYNKILAAKLPRTANEMYHYRRAtiVANRDLRRGDLVFFHIHSRdiADHMGVYLGQG 214
Cdd:PRK10838  79 GVRYRLGG-STKKGIDCSAFVQRTFREQFGLELPRSTYEQQEMGKS--VSRSKLRTGDLVLFRAGST--GRHVGIYIGNN 153

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 696361913 215 QFIE-SPRTGETIrvSNLSDDFWQDHYLGARRILTENT 251
Cdd:PRK10838 154 QFVHaSTSSGVII--SSMNEPYWKKRYNEARRVLSRSS 189
YycO COG3863
Uncharacterized conserved protein YycO, NlpC/P60 family [Function unknown];
126-194 3.05e-03

Uncharacterized conserved protein YycO, NlpC/P60 family [Function unknown];


Pssm-ID: 443072  Cd Length: 166  Bit Score: 37.28  E-value: 3.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696361913 126 AIHRLEQQLGKPYLWGG--TDPDEGFDCSGLIFYAYNKilAAKLPRTANemyhyrRATIVANRDLRRGDLV 194
Cdd:COG3863   97 AANYAYSQVGKPYNYNFvkNVDDKKFYCSQLVWAAYKD--AGGIDLDSN------GGLWVSPDDLLDSPDV 159
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
 161-229 5.43e-03

P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+); Escherichia coli ZntA mediates resistance to toxic levels of selected divalent metal ions. ZntA has the highest selectivity for Pb(2+), followed by Zn(2+) and Cd(2+); it also shows low levels of activity with Cu(2+), Ni(2+), and Co(2+). It is upregulated by the transcription factor ZntR at high zinc concentrations. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319846 [Multi-domain]  Cd Length: 597  Bit Score: 37.77  E-value: 5.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696361913 161 KILAAKLPRTANEMYHYRRATIVANRdLRRGDLVFFHIHSRDIADhmGVYL-GQGQFIESPRTGETIRVS 229
Cdd:cd07546   91 KALMALVPETALREENGERREVPADS-LRPGDVIEVAPGGRLPAD--GELLsGFASFDESALTGESIPVE 157
 
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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