ID   CLPP1_CHLFF             Reviewed;         203 AA.
AC   Q256C2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, 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=CF0094;
OS   Chlamydophila felis (strain Fe/C-56).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H.,
RA   Fukushi H., Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(2006).
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; AP006861; BAE80866.1; -; Genomic_DNA.
DR   RefSeq; YP_515011.1; -.
DR   MEROPS; S14.001; -.
DR   GeneID; 3958766; -.
DR   GenomeReviews; AP006861_GR; CF0094.
DR   KEGG; cfe:CF0094; -.
DR   HOGENOM; Q256C2; -.
DR   OMA; Q256C2; ANKLCAQ.
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_0000252810.
FT   ACT_SITE     98     98       By similarity.
FT   ACT_SITE    123    123       By similarity.
SQ   SEQUENCE   203 AA;  22105 MW;  1CBEC2AEDB3FD447 CRC64;
     MTLVPYVVED TGRGERAMDI YSRLLKDRIV MIGQEITEPL ANTVIAQLLF LMSEDPQKDI
     KVFINSPGGY ITAGLAIYDT IRFLGCDVNT YCIGQAASMG ALLLSAGTKG KRYALPHSRM
     MIHQPSGGII GTSADIQLQA AEILTLKKHL ANILSECTGQ PVEKIIEDSE RDFFMGAEDA
     ISYGLIDKVV SSAKDTKDKD TIS
//