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Database: UniProt
Entry: Q5HHQ0
LinkDB: Q5HHQ0
Original site: Q5HHQ0 
ID   CLPP_STAAC              Reviewed;         195 AA.
AC   Q5HHQ0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   09-JUL-2014, entry version 67.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
GN   Name=clpP; OrderedLocusNames=SACOL0833;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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   -!- 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 proteasomes
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
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DR   EMBL; CP000046; AAW36389.1; -; Genomic_DNA.
DR   RefSeq; YP_185707.1; NC_002951.2.
DR   ProteinModelPortal; Q5HHQ0; -.
DR   SMR; Q5HHQ0; 4-192.
DR   STRING; 93062.SACOL0833; -.
DR   BindingDB; Q5HHQ0; -.
DR   EnsemblBacteria; AAW36389; AAW36389; SACOL0833.
DR   GeneID; 3238532; -.
DR   KEGG; sac:SACOL0833; -.
DR   PATRIC; 19527918; VBIStaAur112458_0811.
DR   eggNOG; COG0740; -.
DR   HOGENOM; HOG000285833; -.
DR   KO; K01358; -.
DR   OMA; KGERSFD; -.
DR   OrthoDB; EOG6Z3KQ0; -.
DR   BioCyc; SAUR93062:GCEP-823-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN         1    195       ATP-dependent Clp protease proteolytic
FT                                subunit.
FT                                /FTId=PRO_0000179649.
FT   ACT_SITE     98     98       Nucleophile (By similarity).
FT   ACT_SITE    123    123       By similarity.
SQ   SEQUENCE   195 AA;  21514 MW;  811110E32846625E CRC64;
     MNLIPTVIET TNRGERAYDI YSRLLKDRII MLGSQIDDNV ANSIVSQLLF LQAQDSEKDI
     YLYINSPGGS VTAGFAIYDT IQHIKPDVQT ICIGMAASMG SFLLAAGAKG KRFALPNAEV
     MIHQPLGGAQ GQATEIEIAA NHILKTREKL NRILSERTGQ SIEKIQKDTD RDNFLTAEEA
     KEYGLIDEVM VPETK
//
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