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C6UBQ2 (C6UBQ2_ECOBR) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 33. 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 EMBL ACT38078.1
Ordered Locus Names:ECB_00388 EMBL ACT38078.1
OrganismEscherichia coli (strain B / REL606) [Complete proteome] [HAMAP] EMBL ACT38078.1
Taxonomic identifier413997 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length207 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

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 site1111 By similarity HAMAP-Rule MF_00444
Active site1361 By similarity HAMAP-Rule MF_00444

Sequences

Sequence LengthMass (Da)Tools
C6UBQ2 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: A7843D036C8CB3C2

FASTA20723,187
        10         20         30         40         50         60 
MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE DHMANLIVAQ 

        70         80         90        100        110        120 
MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD VSTICMGQAA SMGAFLLTAG 

       130        140        150        160        170        180 
AKGKRFCLPN SRVMIHQPLG GYQGQATDIE IHAREILKVK GRMNELMALH TGQSLEQIER 

       190        200 
DTERDRFLSA PEAVEYGLVD SILTHRN 

« Hide

References

[1]"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)."
Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.
J. Mol. Biol. 394:644-652(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / REL606.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000819 Genomic DNA. Translation: ACT38078.1.
RefSeqYP_003043614.1. NC_012967.1.

3D structure databases

ProteinModelPortalC6UBQ2.
SMRC6UBQ2. Positions 16-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413997.ECB_00388.

Proteomic databases

PRIDEC6UBQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT38078; ACT38078; ECB_00388.
GeneID8175309.
KEGGebr:ECB_00388.
PATRIC18232732. VBIEscCol118196_0418.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECOL413997:GCQD-574-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 nameC6UBQ2_ECOBR
AccessionPrimary (citable) accession number: C6UBQ2
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: February 19, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)