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 01-MAY-2013, entry version 59.
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 -!- 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 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; LVHPPQA; -.
DR ProtClustDB; PRK00277; -.
DR BindingDB; Q5HHQ0; -.
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; 1.
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 1 195 ATP-dependent Clp protease proteolytic
FT subunit.
FT /FTId=PRO_0000179649.
FT ACT_SITE 98 98 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
//
