ID   CLPP1_CHLT2             Reviewed;         192 AA.
AC   B0B803;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
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=CTL0690;
OS   Chlamydia trachomatis (strain L2/434/Bu / ATCC VR902B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=471472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J.,
RA   Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H.,
RA   Harris B., Ormond D., Rance R., Quail M.A., Parkhill J.,
RA   Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-11.
RA   Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M.,
RA   Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G.,
RA   Pallini V.;
RL   Submitted (SEP-1994) to UniProtKB.
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; AM884176; CAP04129.1; -; Genomic_DNA.
DR   RefSeq; YP_001654762.1; -.
DR   GeneID; 5858690; -.
DR   GenomeReviews; AM884176_GR; CTL0690.
DR   KEGG; ctb:CTL0690; -.
DR   OMA; B0B803; TPHSRIM.
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   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Hydrolase; Nucleotide-binding; Protease; Serine protease.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    192       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000340090.
FT   ACT_SITE     92     92       By similarity.
FT   ACT_SITE    117    117       By similarity.
FT   CONFLICT      8      8       H -> M (in Ref. 2; AA sequence).
SQ   SEQUENCE   192 AA;  21073 MW;  589EF06C344F20EF CRC64;
     MPEGEMMHKL QDVIDRKLLD SRRIFFSEPV TEKSAAEAIK KLWYLELTNP GQPIVFVINS
     PGGSVDAGFA VWDQIKMISS PLTTVVTGLA ASMGSVLSLC AVPGRRFATP HARIMIHQPS
     IGGTITGQAT DLDIHAREIL KTKARIIDVY VEATGQSPEV IEKAIDRDMW MSANEAMEFG
     LLDGILFSFN DL
//