ID   CLPP1_PROMT             Reviewed;         196 AA.
AC   Q46L44;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=PMN2A_0292;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Prochlorophytes; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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; CP000095; AAZ57784.1; -; Genomic_DNA.
DR   RefSeq; YP_291487.1; -.
DR   GeneID; 3605664; -.
DR   GenomeReviews; CP000095_GR; PMN2A_0292.
DR   KEGG; pmn:PMN2A_0292; -.
DR   HOGENOM; Q46L44; -.
DR   OMA; Q46L44; MIPIVIE.
DR   BioCyc; PMAR59920:PMN2A_0292-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   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    196       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000226456.
FT   ACT_SITE     96     96       By similarity.
FT   ACT_SITE    121    121       By similarity.
SQ   SEQUENCE   196 AA;  21824 MW;  3FB83FFD0AC1489C CRC64;
     MIPIVIEESG RGERAFDIYS RLLRERIVFL GEPVTSDSAN RIVAQLLFLE ADDPDKDIFL
     YINSPGGSVY DGLGIFDTMQ HVKPDIHTVC VGLAASMGAF LLCAGAKGKR SSLLHSRIMI
     HQPLGGARGQ ASDIRIQADE ILFIKDKLNK ELSDRTGQPI ERIREDTDRD FYMSPSEAIE
     YGIIDNVFNK RPINSV
//