CLPP_SALTY
ID CLPP_SALTY Reviewed; 207 AA.
AC P0A1D7; Q9LC07;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=STM0448;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=x3306;
RX PubMed=11292737; DOI=10.1128/iai.69.5.3164-3174.2001;
RA Yamamoto T., Sashinami H., Takaya A., Tomoyasu T., Matsui H., Kikuchi Y.,
RA Hanawa T., Kamiya S., Nakane A.;
RT "Disruption of the genes for ClpXP protease in Salmonella enterica serovar
RT Typhimurium results in persistent infection in mice, and development of
RT persistence requires endogenous gamma interferon and tumor necrosis factor
RT alpha.";
RL Infect. Immun. 69:3164-3174(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
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DR EMBL; AB033628; BAA94668.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19403.1; -; Genomic_DNA.
DR RefSeq; NP_459444.1; NC_003197.2.
DR RefSeq; WP_000122257.1; NC_003197.2.
DR AlphaFoldDB; P0A1D7; -.
DR SMR; P0A1D7; -.
DR STRING; 99287.STM0448; -.
DR MEROPS; S14.001; -.
DR PaxDb; P0A1D7; -.
DR EnsemblBacteria; AAL19403; AAL19403; STM0448.
DR GeneID; 1251968; -.
DR GeneID; 66754911; -.
DR KEGG; stm:STM0448; -.
DR PATRIC; fig|99287.12.peg.480; -.
DR HOGENOM; CLU_058707_3_2_6; -.
DR OMA; RDYWMKA; -.
DR PhylomeDB; P0A1D7; -.
DR BioCyc; SENT99287:STM0448-MON; -.
DR PHI-base; PHI:3040; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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;
KW Zymogen.
FT PROPEP 1..14
FT /evidence="ECO:0000250"
FT /id="PRO_0000268020"
FT CHAIN 15..207
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179645"
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
