ID   CLPP1_CHLTA             Reviewed;         192 AA.
AC   Q3KLR9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=CTA_0471;
OS   Chlamydia trachomatis (strain A/HAR-13 / ATCC VR-571B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177312; DOI=10.1128/IAI.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(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; CP000051; AAX50703.1; -; Genomic_DNA.
DR   RefSeq; YP_328251.1; -.
DR   GeneID; 3687344; -.
DR   GenomeReviews; CP000051_GR; CTA_0471.
DR   KEGG; cta:CTA_0471; -.
DR   HOGENOM; Q3KLR9; -.
DR   OMA; Q3KLR9; TPHSRIM.
DR   BioCyc; CTRA315277-1:CTA_0471-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; FALSE_NEG.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
FT   CHAIN         1    192       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000226435.
FT   ACT_SITE     92     92       By similarity.
FT   ACT_SITE    117    117       By similarity.
SQ   SEQUENCE   192 AA;  21162 MW;  33EEEE8CD3B8AACE CRC64;
     MPEGEMMHKL QDVIDRKLLD SRRIFFSEPV TEKSATEAIK KLWYLELTNP GQPIVFVINS
     PGGSVDAGFA VWDQIKMISS PLTTVVTGLA ASMGSVLSLC AVPGRRFATP HARIMIHQPS
     IGGTITGQAT DLDIHAREIL KTKARIIDVY VEATGQSREV IEKAIDRDMW MSANEAMEFG
     LLDGILFSFN DL
//