ID   CLPP_SALCH              Reviewed;         207 AA.
AC   Q57SB5;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 109.
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};
DE   Flags: Precursor;
GN   Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=SCH_0490;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(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.
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. Component of the
CC       ClpAP and ClpXP complexes. {ECO:0000255|HAMAP-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX64396.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017220; AAX64396.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000122257.1; NC_006905.1.
DR   AlphaFoldDB; Q57SB5; -.
DR   SMR; Q57SB5; -.
DR   MEROPS; S14.001; -.
DR   EnsemblBacteria; AAX64396; AAX64396; SCH_0490.
DR   GeneID; 66754911; -.
DR   KEGG; sec:SCH_0490; -.
DR   HOGENOM; CLU_058707_3_3_6; -.
DR   Proteomes; UP000000538; 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; Serine protease; Zymogen.
FT   PROPEP          1..14
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000268017"
FT   CHAIN           15..207
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000179642"
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   207 AA;  23177 MW;  91D89AC16428F988 CRC64;
     MSYSGERDNL APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE DHMANLIVAQ
     MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD VSTICMGQAA SMGAFLLTAG
     AKGKRFCLPN SRVMIHQPLG GYQGQATDIE IHAREILKVK GRMNELMAHH TGQSLEQIER
     DTERDRFLSA PEAVEYGLVD SILTHRN