ID   CLPP1_RHIEC             Reviewed;         202 AA.
AC   Q2KAB9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit 1;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp 1;
GN   Name=clpP1; OrderedLocusNames=RHE_CH01414;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic
RT   redundancy in seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC90217.1; -; Genomic_DNA.
DR   RefSeq; YP_468944.1; -.
DR   GeneID; 3892971; -.
DR   GenomeReviews; CP000133_GR; RHE_CH01414.
DR   KEGG; ret:RHE_CH01414; -.
DR   HOGENOM; Q2KAB9; -.
DR   OMA; Q2KAB9; LYAEHCG.
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; -; 1.
DR   InterPro; IPR001907; Pept_S14_ClpP.
DR   InterPro; IPR018215; Pept_S14_ClpP_CS.
DR   PANTHER; PTHR10381; Pept_S14_ClpP; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; FALSE_NEG.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
FT   CHAIN         1    202       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000252832.
FT   ACT_SITE    101    101       By similarity.
FT   ACT_SITE    126    126       By similarity.
SQ   SEQUENCE   202 AA;  22721 MW;  C8BB5CE396B0CFE3 CRC64;
     MREAMQLVPM VIEQSSRGER SFDIYSRLLR ERIIFLNGEV NDTVSALVCA QLLFLEADPE
     KPINLYINSP GGAVTSGLAM YDTMRFIRAP VHTLCMGTAR SMGSFLLMAG EPGERAALPN
     ASILIHQPSG GFQGQASDML IHAEEILKTK QRMTRLYAEH CGRSYEDFER GMDRDRFMTA
     EEALEWGLIE RILKVREDTS SL
//