ID   CLPP1_SALRD             Reviewed;         233 AA.
AC   Q2S2L8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   16-JUN-2009, entry version 27.
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=SRU_1439;
OS   Salinibacter ruber (strain DSM 13855).
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J.,
RA   Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G.,
RA   Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F.,
RA   Charlebois R.L., Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(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; CP000159; ABC44393.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_445563.1; -.
DR   MEROPS; S14.001; -.
DR   GeneID; 3851308; -.
DR   GenomeReviews; CP000159_GR; SRU_1439.
DR   KEGG; sru:SRU_1439; -.
DR   NMPDR; fig|309807.5.peg.1357; -.
DR   TIGR; SRU_1439; -.
DR   HOGENOM; Q2S2L8; -.
DR   BioCyc; SRUB309807:SRU_1439-MON; -.
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; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
FT   CHAIN         1    233       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000236402.
FT   ACT_SITE    116    116       By similarity.
FT   ACT_SITE    141    141       By similarity.
SQ   SEQUENCE   233 AA;  25299 MW;  150EA6B8A86FF59C CRC64;
     MTSLPSSIFQ GGLGDQPQSG LVPKVVEQTT RGERAYDIFS RLLKERIVFI GTPINDQIAN
     LTVAQLLYLE SEGSSQPINI YINSPGGVIY SGLGVYDTMQ YVEAPISTTC VGLAASMGSV
     LLAGGEDGQR ACLPNSRVMM HQPMGGTEGQ ASDIEIQAKE MAWLKKRLYQ ILSFHTGKDI
     DQIEEDADRN HWLSAEEAQE YGLVDQVMNE GNLDALKSIH ANGEASDADS DEE
//