CLPP_STAA8
ID CLPP_STAA8 Reviewed; 195 AA.
AC Q2G036;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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};
GN OrderedLocusNames=SAOUHSC_00790;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD29919.1; -; Genomic_DNA.
DR RefSeq; WP_001049165.1; NZ_LS483365.1.
DR RefSeq; YP_499347.1; NC_007795.1.
DR PDB; 3QWD; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-195.
DR PDB; 3V5E; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-195.
DR PDB; 3V5I; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=1-195.
DR PDB; 4MXI; X-ray; 2.30 A; A/B/C/D/E/F/G=1-195.
DR PDB; 5C90; X-ray; 1.75 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-195.
DR PDB; 5VZ2; X-ray; 2.26 A; A/B/C/D/E/F/G/I/K/L/M/N/S/T=1-195.
DR PDB; 5W18; X-ray; 2.44 A; A/B/C/D/E/F/G/I/K/L/M/N/S/T=1-195.
DR PDB; 6DKF; EM; 3.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-195.
DR PDB; 6L3X; X-ray; 2.31 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=19-195.
DR PDB; 6L40; X-ray; 2.21 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=19-193.
DR PDB; 6N80; X-ray; 1.96 A; A/B/C/D/E/F/G/I/K/L/M/N/S/T=1-195.
DR PDB; 6PKA; X-ray; 2.25 A; A/B/C/D/E/F/G/I/K/L/M/N/S/T=1-195.
DR PDB; 6PMD; X-ray; 2.21 A; A/B/C/D/E/F/G/I/K/L/M/N/S/T=1-195.
DR PDB; 6TTY; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-195.
DR PDB; 6TTZ; X-ray; 2.20 A; A/B/C/D/E/F/G=1-195.
DR PDBsum; 3QWD; -.
DR PDBsum; 3V5E; -.
DR PDBsum; 3V5I; -.
DR PDBsum; 4MXI; -.
DR PDBsum; 5C90; -.
DR PDBsum; 5VZ2; -.
DR PDBsum; 5W18; -.
DR PDBsum; 6DKF; -.
DR PDBsum; 6L3X; -.
DR PDBsum; 6L40; -.
DR PDBsum; 6N80; -.
DR PDBsum; 6PKA; -.
DR PDBsum; 6PMD; -.
DR PDBsum; 6TTY; -.
DR PDBsum; 6TTZ; -.
DR AlphaFoldDB; Q2G036; -.
DR SMR; Q2G036; -.
DR STRING; 1280.SAXN108_0836; -.
DR BindingDB; Q2G036; -.
DR ChEMBL; CHEMBL1932910; -.
DR MEROPS; S14.001; -.
DR EnsemblBacteria; ABD29919; ABD29919; SAOUHSC_00790.
DR GeneID; 3919354; -.
DR GeneID; 66839059; -.
DR KEGG; sao:SAOUHSC_00790; -.
DR PATRIC; fig|93061.5.peg.713; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_3_2_9; -.
DR OMA; GFKRQDP; -.
DR BRENDA; 3.4.21.92; 3352.
DR EvolutionaryTrace; Q2G036; -.
DR PRO; PR:Q2G036; -.
DR Proteomes; UP000008816; 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..195
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000252851"
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 STRAND 6..10
FT /evidence="ECO:0007829|PDB:6TTY"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:6TTY"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5C90"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5C90"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:5C90"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:5C90"
FT HELIX 133..158
FT /evidence="ECO:0007829|PDB:5C90"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5C90"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:5C90"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5C90"
SQ SEQUENCE 195 AA; 21514 MW; 811110E32846625E CRC64;
MNLIPTVIET TNRGERAYDI YSRLLKDRII MLGSQIDDNV ANSIVSQLLF LQAQDSEKDI
YLYINSPGGS VTAGFAIYDT IQHIKPDVQT ICIGMAASMG SFLLAAGAKG KRFALPNAEV
MIHQPLGGAQ GQATEIEIAA NHILKTREKL NRILSERTGQ SIEKIQKDTD RDNFLTAEEA
KEYGLIDEVM VPETK
