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 01-MAY-2013, entry version 40.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE EC=3.4.21.92;
DE AltName: Full=Endopeptidase Clp;
GN Name=clpP; 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 (By
CC similarity).
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase S14 family.
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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; LVHPPQA; -.
DR ProtClustDB; PRK00277; -.
DR BioCyc; CVES412965:GHZZ-197-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA:HAMAP.
DR HAMAP; MF_00444; ClpP; 1; -.
DR InterPro; IPR001907; ClpP.
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 TIGRFAMs; TIGR00493; clpP; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; FALSE_NEG.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW Nucleotide-binding; Protease; Serine protease.
FT CHAIN 1 198 ATP-dependent Clp protease proteolytic
FT subunit.
FT /FTId=PRO_1000026144.
FT ACT_SITE 103 103 By similarity.
FT ACT_SITE 128 128 By similarity.
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
//
