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B1JTV0 (B1JTV0_BURCC) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease proteolytic subunit HAMAP-Rule MF_00444 RuleBase RU003567

EC=3.4.21.92 HAMAP-Rule MF_00444 RuleBase RU000549
Alternative name(s):
Endopeptidase Clp HAMAP-Rule MF_00444
Gene names
Name:clpP HAMAP-Rule MF_00444
Ordered Locus Names:Bcenmc03_1946 EMBL ACA91107.1
OrganismBurkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP] EMBL ACA91107.1
Taxonomic identifier406425 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins By similarity. HAMAP-Rule MF_00444 RuleBase RU000550

Catalytic activity

Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). HAMAP-Rule MF_00444

Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu-and -Tyr-|-Trp bonds also occurs). RuleBase RU000549

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00444.

Sequence similarities

Belongs to the peptidase S14 family. HAMAP-Rule MF_00444 RuleBase RU003567

Ontologies

Keywords
   Cellular componentCytoplasm HAMAP-Rule MF_00444
   LigandATP-binding HAMAP-Rule MF_00444
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease HAMAP-Rule MF_00444 RuleBase RU000549
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1211 By similarity HAMAP-Rule MF_00444
Active site1461 By similarity HAMAP-Rule MF_00444

Sequences

Sequence LengthMass (Da)Tools
B1JTV0 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 924F3B6062C85117

FASTA21723,750
        10         20         30         40         50         60 
MITRAELLDM LASNAPQGFE AQALGLVPIV VETSGRGERS YDIYSRLLKE RLVFMVGEVN 

        70         80         90        100        110        120 
DQTANLVVAQ LLFLESENPD KDISLYINSP GGSVSAGMAI YDTMQFIKPD VSTLCMGLAA 

       130        140        150        160        170        180 
SMGAFLLASG AKGKRFALPN SRVMIHQPLG GARGQASDIE IQAREILYLK ERLNNLLAQH 

       190        200        210 
TGQDVERIAR DTDRDNFMSS EDAKAYGLID QVLLKRP 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3."
Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Tiedje J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC0-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000958 Genomic DNA. Translation: ACA91107.1.
RefSeqYP_001765229.1. NC_010508.1.

3D structure databases

ProteinModelPortalB1JTV0.
SMRB1JTV0. Positions 25-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING406425.Bcenmc03_1946.

Protein family/group databases

MEROPSS14.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA91107; ACA91107; Bcenmc03_1946.
GeneID6123610.
KEGGbcm:Bcenmc03_1946.
PATRIC19091005. VBIBurCen61509_2008.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0740.
HOGENOMHOG000285833.
KOK01358.
OMAANLIIAQ.
OrthoDBEOG6Z3KQ0.
ProtClustDBPRK00277.

Enzyme and pathway databases

BioCycBCEN406425:GHD9-1996-MONOMER.

Family and domain databases

HAMAPMF_00444. ClpP.
InterProIPR001907. ClpP.
IPR023562. ClpP/TepA.
IPR018215. ClpP_AS.
[Graphical view]
PANTHERPTHR10381. PTHR10381. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
TIGRFAMsTIGR00493. clpP. 1 hit.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB1JTV0_BURCC
AccessionPrimary (citable) accession number: B1JTV0
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)