CLPP_CAMJE
ID CLPP_CAMJE Reviewed; 194 AA.
AC P54413; Q0PBU7; Q9PIT7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=Cj0192c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=7670637; DOI=10.1099/13500872-141-6-1359;
RA Griffiths P.L., Park R.W.A., Connerton I.F.;
RT "The gene for Campylobacter trigger factor: evidence for multiple
RT transcription start sites and protein products.";
RL Microbiology 141:1359-1367(1995).
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; AL111168; CAL34361.1; -; Genomic_DNA.
DR EMBL; X85954; CAA59932.1; -; Genomic_DNA.
DR PIR; G81437; G81437.
DR RefSeq; WP_002806309.1; NC_002163.1.
DR RefSeq; YP_002343650.1; NC_002163.1.
DR AlphaFoldDB; P54413; -.
DR SMR; P54413; -.
DR IntAct; P54413; 97.
DR STRING; 192222.Cj0192c; -.
DR MEROPS; S14.001; -.
DR PaxDb; P54413; -.
DR PRIDE; P54413; -.
DR EnsemblBacteria; CAL34361; CAL34361; Cj0192c.
DR GeneID; 906014; -.
DR KEGG; cje:Cj0192c; -.
DR PATRIC; fig|192222.6.peg.189; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_3_2_7; -.
DR OMA; RDYWMKA; -.
DR Proteomes; UP000000799; 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 InterPro; IPR018215; ClpP_Ser_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00493; clpP; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..194
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179524"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 122
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 194 AA; 21650 MW; E0B520BD0398093D CRC64;
MFIPYVIEKS SRGERSYDIY SRLLKDRIIM LSGEIHDELA ASIVAQLLFL EAEDPTKDIY
LYINSPGGVI TSGFSIYDTM NYIKPDVCTI CIGQAASMGA FLLSCGAEGK RFALPNSRIM
IHQPLGGARG QATDIEIQAK EILRLKTILN DILAKNTKQK VAKIAKDTER DFFMSAQEAK
EYGLIDKVLE KSFK
