ID   CLPP1_BORBU             Reviewed;         197 AA.
AC   O51556;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
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; Synonyms=clpP-1; OrderedLocusNames=BB_0611;
OS   Borrelia burgdorferi (Lyme disease spirochete).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE000783; AAC66964.1; -; Genomic_DNA.
DR   PIR; B70176; B70176.
DR   RefSeq; NP_212745.1; -.
DR   HSSP; P19245; 1TYF.
DR   GeneID; 1195460; -.
DR   GenomeReviews; AE000783_GR; BB_0611.
DR   KEGG; bbu:BB0611; -.
DR   NMPDR; fig|224326.1.peg.995; -.
DR   TIGR; BB_0611; -.
DR   HOGENOM; O51556; -.
DR   OMA; O51556; PDIVTIC.
DR   BioCyc; BBUR224326:BB_0611-MON; -.
DR   BRENDA; 3.4.21.92; 142596.
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   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    197       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000179509.
FT   ACT_SITE    102    102       By similarity.
FT   ACT_SITE    127    127       By similarity.
SQ   SEQUENCE   197 AA;  22064 MW;  5044A9D2053E648A CRC64;
     MEFMHNLIPT VIENTGNYER VFDIYSRLLR ERIIFLSGEI NDPKADTVIA QLLFLESEDS
     SKDIYLYLNS PGGSITAGLA IYDTMQYIKP DVRTICIGQA ASMGAFLLAG GAKGKRESLT
     YSRIMIHQPW GGISGQASDI NIQANEILRL KKLIIDIMSN QIGVDKEKLA LDMERDYFMT
     SSDALKYGLI DSILVRE
//