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C2GTS9 (C2GTS9_BIFLN) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 16. 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 2 HAMAP MF_00444

EC=3.4.21.92 HAMAP MF_00444
Alternative name(s):
Endopeptidase Clp 2 HAMAP MF_00444
Gene names
Name:clpP2 HAMAP MF_00444 EMBL EEI81486.1
ORF Names:HMPREF0175_0426 EMBL EEI81486.1
OrganismBifidobacterium longum subsp. longum ATCC 55813 EMBL EEI81486.1
Taxonomic identifier548480 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

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 MF_00444

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 MF_00444

Subcellular location

Cytoplasm By similarity HAMAP MF_00444.

Sequence similarities

Belongs to the peptidase S14 family. RuleBase RU003567 HAMAP MF_00444

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Ontologies

Keywords
   Cellular componentCytoplasm HAMAP MF_00444
   LigandATP-binding HAMAP MF_00444
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease HAMAP MF_00444
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1021 By similarity HAMAP MF_00444
Active site1271 By similarity HAMAP MF_00444

Sequences

Sequence LengthMass (Da)Tools
C2GTS9 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: B2056BCDBD66B3DB

FASTA20722,724
        10         20         30         40         50         60 
MSNTFATLPV MAGDDVPAGP VDPIFNRLLK DRIIWMGEEV KDDMANRICA QLLMLAAEDP 

        70         80         90        100        110        120 
KKDIWLYINS PGGSITAGMA IYDTMQLIEP DVATVGLGMC ASMGQFLLSS GTKGKRYLTS 

       130        140        150        160        170        180 
HARVLMHQPS GGIGGTATDV RINAELIMDM KKTMSELTAE QTGHTLEEIY RDNEYDHWFT 

       190        200 
AQEALDYGFV DKLVTTPDTI GNNQQGE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACHI01000008 Genomic DNA. Translation: EEI81486.1.

3D structure databases

ProteinModelPortalC2GTS9.
SMRC2GTS9. Positions 23-196.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC36941652. VBIBifLon7869_0418.

Family and domain databases

HAMAPMF_00444. ClpP.
[Tree]
InterProIPR023562. Pept_S14/S49.
IPR001907. Pept_S14_ClpP.
[Graphical view]
PANTHERPTHR10381. Pept_S14_ClpP. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
ProtoNetSearch...

Entry information

Entry nameC2GTS9_BIFLN
AccessionPrimary (citable) accession number: C2GTS9
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)