CLPP1_CHLPN
ID CLPP1_CHLPN Reviewed; 191 AA.
AC Q9Z832; Q9JQ83;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp 1 {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP1 {ECO:0000255|HAMAP-Rule:MF_00444}; Synonyms=clp;
GN OrderedLocusNames=CPn_0520, CP_0233, CpB0541;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins to small peptides in the presence of
CC ATP and magnesium. alpha-casein is the usual test substrate. In the
CC absence of ATP, only oligopeptides shorter than five residues are
CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444};
CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC stack back to back to give a disk-like structure with a central cavity,
CC resembling the structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
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DR EMBL; AE001363; AAD18660.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38099.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98726.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98470.1; -; Genomic_DNA.
DR PIR; D86555; D86555.
DR PIR; G72067; G72067.
DR RefSeq; NP_224716.1; NC_000922.1.
DR RefSeq; WP_010883158.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z832; -.
DR SMR; Q9Z832; -.
DR STRING; 115711.CP_0233; -.
DR MEROPS; S14.005; -.
DR EnsemblBacteria; AAD18660; AAD18660; CPn_0520.
DR EnsemblBacteria; AAF38099; AAF38099; CP_0233.
DR GeneID; 45050562; -.
DR KEGG; cpa:CP_0233; -.
DR KEGG; cpj:clpP_1; -.
DR KEGG; cpn:CPn_0520; -.
DR KEGG; cpt:CpB0541; -.
DR PATRIC; fig|115713.3.peg.579; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_4_0_0; -.
DR OMA; RFIQPHA; -.
DR OrthoDB; 1728970at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd07017; S14_ClpP_2; 1.
DR HAMAP; MF_00444; ClpP; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR033135; ClpP_His_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Serine protease.
FT CHAIN 1..191
FT /note="ATP-dependent Clp protease proteolytic subunit 1"
FT /id="PRO_0000179532"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 116
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 191 AA; 21020 MW; 56F801EF1469C037 CRC64;
MADGEVHKLR DIIEKELLEA RRVFFSEPVT EKSASDAIKK LWYLELKDPG KPIVFVINSP
GGSVDAGFAV WDQIKMLTSP VTTVVTGLAA SMGSVLSLCA APGRRFATPH SRIMIHQPSI
GGPITGQATD LDIHAREILK TKARIIDVYV EATNQPRDII EKAIDRDMWM TANEAKDFGL
LDGILFSFND L
