CLPP_LACLM
ID CLPP_LACLM Reviewed; 199 AA.
AC Q9ZAB0; A2RIZ2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 119.
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=llmg_0638;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9987112; DOI=10.1046/j.1365-2958.1999.01149.x;
RA Frees D., Ingmer H.;
RT "ClpP participates in the degradation of misfolded protein in Lactococcus
RT lactis.";
RL Mol. Microbiol. 31:79-87(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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 -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
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DR EMBL; AF028804; AAD01866.2; -; Genomic_DNA.
DR EMBL; AM406671; CAL97240.1; -; Genomic_DNA.
DR RefSeq; WP_011834647.1; NZ_WJVF01000023.1.
DR AlphaFoldDB; Q9ZAB0; -.
DR SMR; Q9ZAB0; -.
DR STRING; 416870.llmg_0638; -.
DR MEROPS; S14.001; -.
DR EnsemblBacteria; CAL97240; CAL97240; llmg_0638.
DR GeneID; 60355638; -.
DR GeneID; 61108933; -.
DR KEGG; llm:llmg_0638; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_3_2_9; -.
DR OMA; RDYWMKA; -.
DR PhylomeDB; Q9ZAB0; -.
DR BioCyc; LLAC416870:LLMG_RS03330-MON; -.
DR BRENDA; 3.4.21.92; 2903.
DR Proteomes; UP000000364; 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:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:CACAO.
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 PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Protease; Serine protease; Stress response.
FT CHAIN 1..199
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179574"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 124
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 199 AA; 22052 MW; F2CC13835891CCFF CRC64;
MGYLVPTVIE QSSRGERAYD IYSRLLKDRI IMLTGPVEDG MANSIIAQLL FLDAQDNTKD
IYLYVNTPGG SVSAGLAIVD TMNFIKSDVQ TIVMGMAASM GTIIASSGTK GKRFMLPNAE
YLIHQPMGGA GQGTQQTDMA IVAEQLLKTR KRLEQILADN SNRSLEQIHK DAERDHWMDA
KETLEYGFID EIMENNSLK
