ID CLPP_BORGA Reviewed; 194 AA.
AC Q660R2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 57.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE EC=3.4.21.92;
DE AltName: Full=Endopeptidase Clp;
GN Name=clpP; OrderedLocusNames=BG0627;
OS Borrelia garinii (strain PBi).
OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC Borrelia burgdorferi group.
OX NCBI_TaxID=290434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBi;
RX PubMed=15547252; DOI=10.1093/nar/gkh953;
RA Gloeckner G., Lehmann R., Romualdi A., Pradella S.,
RA Schulte-Spechtel U., Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT "Comparative analysis of the Borrelia garinii genome.";
RL Nucleic Acids Res. 32:6038-6046(2004).
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; CP000013; AAU07459.1; -; Genomic_DNA.
DR RefSeq; YP_073051.1; NC_006156.1.
DR ProteinModelPortal; Q660R2; -.
DR SMR; Q660R2; 4-191.
DR STRING; 290434.BG0627; -.
DR MEROPS; S14.001; -.
DR EnsemblBacteria; AAU07459; AAU07459; BG0627.
DR GeneID; 2957855; -.
DR KEGG; bga:BG0627; -.
DR PATRIC; 20566823; VBIBorGar102262_0718.
DR HOGENOM; HOG000285833; -.
DR KO; K01358; -.
DR OMA; AGLIMAQ; -.
DR ProtClustDB; PRK00277; -.
DR BioCyc; BGAR290434:BG0627-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; 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 1 194 ATP-dependent Clp protease proteolytic
FT subunit.
FT /FTId=PRO_0000179511.
FT ACT_SITE 99 99 By similarity.
FT ACT_SITE 124 124 By similarity.
SQ SEQUENCE 194 AA; 21734 MW; 49D88A707366A914 CRC64;
MHNLIPTVIE HTGNYERVFD IYSRLLRERI IFLSGEINDL KADTVIAQLL FLESEDSNKD
IYLYLNSPGG SITAGLAIYD TMQYIKPDVR TICIGQAASM GAFLLAGGAK GKRESLAYSR
IMIHQPWGGI SGQASDINIQ ANEILRLKKL IIDIMSNQIG IDKEKLALDM ERDYFMTSND
ALKYGLIDSI LVRE
//
