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Database: UniProt
Entry: A5CXJ8
LinkDB: A5CXJ8
Original site: A5CXJ8 
ID   CLPP_VESOH              Reviewed;         198 AA.
AC   A5CXJ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   26-NOV-2014, entry version 51.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
DE            EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE   AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
GN   Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444};
GN   OrderedLocusNames=COSY_0203;
OS   Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria;
OC   sulfur-oxidizing symbionts.
OX   NCBI_TaxID=412965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA;
RX   PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA   Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA   Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y.,
RA   Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.;
RT   "Reduced genome of the thioautotrophic intracellular symbiont in a
RT   deep-sea clam, Calyptogena okutanii.";
RL   Curr. Biol. 17:881-886(2007).
CC   -!- FUNCTION: Cleaves peptides in various proteins in a process that
CC       requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
CC       major role in the degradation of misfolded proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_00444}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
CC       the presence of ATP and magnesium. Alpha-casein is the usual test
CC       substrate. In the absence of ATP, only oligopeptides shorter than
CC       five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
CC       and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu-
CC       and -Tyr-|-Trp bonds also occurs). {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings
CC       which stack back to back to give a disk-like structure with a
CC       central cavity, resembling the structure of eukaryotic
CC       proteasomes. {ECO:0000255|HAMAP-Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00444}.
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DR   EMBL; AP009247; BAF61333.1; -; Genomic_DNA.
DR   RefSeq; YP_001219057.1; NC_009465.1.
DR   ProteinModelPortal; A5CXJ8; -.
DR   SMR; A5CXJ8; 9-198.
DR   STRING; 412965.COSY_0203; -.
DR   MEROPS; S14.001; -.
DR   EnsemblBacteria; BAF61333; BAF61333; COSY_0203.
DR   GeneID; 5172004; -.
DR   KEGG; vok:COSY_0203; -.
DR   PATRIC; 32020221; VBICanVes128383_0200.
DR   eggNOG; COG0740; -.
DR   HOGENOM; HOG000285833; -.
DR   KO; K01358; -.
DR   OMA; GHTIERI; -.
DR   OrthoDB; EOG6Z3KQ0; -.
DR   BioCyc; CVES412965:GHZZ-203-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.226.10; -; 1.
DR   HAMAP; MF_00444; ClpP; 1.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR023562; ClpP/TepA.
DR   InterPro; IPR018215; ClpP_AS.
DR   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00493; clpP; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN         1    198       ATP-dependent Clp protease proteolytic
FT                                subunit.
FT                                /FTId=PRO_1000026144.
FT   ACT_SITE    103    103       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00444}.
FT   ACT_SITE    128    128       {ECO:0000255|HAMAP-Rule:MF_00444}.
SQ   SEQUENCE   198 AA;  21880 MW;  7B8727F548D6638A CRC64;
     MNIKNLNQIP IVVEQSARGE RAYDIYSRLL KERIIFLVGP IEDYMANVVV AQLLFLESEN
     PDKDIHLYIN SPGGSVSAGL AIYDTMQFIK SDISTLCIGQ AASMGALLLT AGTKGKRFAL
     PNVRCMIHQP LGGFSGQASD VDIHAQEILK VRANLNQIFK LHTGQVIKTI QKDTDRDNFM
     SADEATKYGL IDKVLAKR
//
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