ID   CLPP1_SYNJA             Reviewed;         203 AA.
AC   Q2JWJ1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=CYA_0659;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium
OS   Yellowstone A-Prime).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M.,
RA   Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community
RT   revealed by comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000239; ABC98872.1; -; Genomic_DNA.
DR   RefSeq; YP_474135.1; -.
DR   MEROPS; S14.001; -.
DR   GeneID; 3897296; -.
DR   GenomeReviews; CP000239_GR; CYA_0659.
DR   KEGG; cya:CYA_0659; -.
DR   TIGR; CYA_0659; -.
DR   HOGENOM; Q2JWJ1; -.
DR   OMA; Q2JWJ1; NVIRIVA.
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    203       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000236414.
FT   ACT_SITE    101    101       By similarity.
FT   ACT_SITE    126    126       By similarity.
SQ   SEQUENCE   203 AA;  22609 MW;  DD8EC63C2E5E86FE CRC64;
     MPIGVPRVPY RLPGEPYSQW ISLDDRLYQE RILFIGEPID DNLANTIVGV MLYLNSQDPQ
     KDIVMYINSP GGSVTAGMAI YDTMNHVKPD IVTVCVGQAA SMGAFLLAAG TKGKRFALPH
     SRIMLHQPSL GMIQGQASDI EIRARETLRV KRRMNELLAQ MTGQPLEKIE RDVERDFYLS
     ATEAQAYGIV DRVIQERSEA MAG
//