CLPP_LISMO
ID CLPP_LISMO Reviewed; 198 AA.
AC Q9RQI6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=lmo2468;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=10760131; DOI=10.1046/j.1365-2958.2000.01773.x;
RA Gaillot O., Pellegrini E., Bregenholt S., Nair S., Berche P.;
RT "The ClpP serine protease is essential for the intracellular parasitism and
RT virulence of Listeria monocytogenes.";
RL Mol. Microbiol. 35:1286-1294(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(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. {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; AF102775; AAF04744.1; -; Genomic_DNA.
DR EMBL; AL591983; CAD00546.1; -; Genomic_DNA.
DR PIR; AD1383; AD1383.
DR RefSeq; NP_465991.1; NC_003210.1.
DR RefSeq; WP_003722600.1; NZ_CP023861.1.
DR PDB; 4JCT; X-ray; 2.60 A; A/B/C/D/E/F/G=1-198.
DR PDB; 4RYF; X-ray; 2.80 A; H/I/J/K/L/M/N=1-198.
DR PDB; 6SFX; EM; 4.00 A; H/I/J/K/L/M/N=1-198.
DR PDBsum; 4JCT; -.
DR PDBsum; 4RYF; -.
DR PDBsum; 6SFX; -.
DR AlphaFoldDB; Q9RQI6; -.
DR SMR; Q9RQI6; -.
DR STRING; 169963.lmo2468; -.
DR MEROPS; S14.001; -.
DR PaxDb; Q9RQI6; -.
DR EnsemblBacteria; CAD00546; CAD00546; CAD00546.
DR GeneID; 987364; -.
DR KEGG; lmo:lmo2468; -.
DR PATRIC; fig|169963.11.peg.2527; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_3_2_9; -.
DR OMA; GFKRQDP; -.
DR PhylomeDB; Q9RQI6; -.
DR BioCyc; LMON169963:LMO2468-MON; -.
DR Proteomes; UP000000817; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..198
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179586"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:4JCT"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4JCT"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4JCT"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:4JCT"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4JCT"
FT TURN 127..132
FT /evidence="ECO:0007829|PDB:4JCT"
FT HELIX 136..158
FT /evidence="ECO:0007829|PDB:4JCT"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4RYF"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:4JCT"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4JCT"
SQ SEQUENCE 198 AA; 21619 MW; DEFE9F4FF1140CEA CRC64;
MNLIPTVIEQ TSRGERAYDI YSRLLKDRII MLGSAIDDNV ANSIVSQLLF LDAQDPEKDI
FLYINSPGGS ISAGMAIYDT MNFVKADVQT IGMGMAASMG SFLLTAGANG KRFALPNAEI
MIHQPLGGAQ GQATEIEIAA RHILKIKERM NTIMAEKTGQ PYEVIARDTD RDNFMTAQEA
KDYGLIDDII INKSGLKG
