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Conserved domains on  [gi|1801549407|ref|WP_161172955|]
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hypothetical protein [Eggerthella sp. BIOML-A5]

Protein Classification

cysteine peptidase family C39 domain-containing protein( domain architecture ID 2867)

cysteine peptidase family C39 domain-containing protein, similar to Niallia circulans butirosin biosynthesis protein H

PubMed:  11517925

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C39_like super family cl00296
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ...
149-220 4.66e-03

Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.


The actual alignment was detected with superfamily member cd02549:

Pssm-ID: 469710 [Multi-domain]  Cd Length: 141  Bit Score: 36.23  E-value: 4.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801549407 149 RSLGSDEALLREaydeIAAGRPTVVHVA----GPYGEHWICLMGYQGVEdpdalsldNFIALDPANGLEVTASYRY 220
Cdd:cd02549    62 RPLTGLLALLRQ----LAAGHPVIVSVNlgvsITPSGHAMVVIGYDRKG--------NVYVNDPGGGRRLVVSFDE 125
 
Name Accession Description Interval E-value
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
149-220 4.66e-03

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 36.23  E-value: 4.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801549407 149 RSLGSDEALLREaydeIAAGRPTVVHVA----GPYGEHWICLMGYQGVEdpdalsldNFIALDPANGLEVTASYRY 220
Cdd:cd02549    62 RPLTGLLALLRQ----LAAGHPVIVSVNlgvsITPSGHAMVVIGYDRKG--------NVYVNDPGGGRRLVVSFDE 125
 
Name Accession Description Interval E-value
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
149-220 4.66e-03

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 36.23  E-value: 4.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801549407 149 RSLGSDEALLREaydeIAAGRPTVVHVA----GPYGEHWICLMGYQGVEdpdalsldNFIALDPANGLEVTASYRY 220
Cdd:cd02549    62 RPLTGLLALLRQ----LAAGHPVIVSVNlgvsITPSGHAMVVIGYDRKG--------NVYVNDPGGGRRLVVSFDE 125
 
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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