CLPP_STAAW
ID CLPP_STAAW Reviewed; 195 AA.
AC P63786; Q99VK9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=MW0730;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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 -!- INTERACTION:
CC P63786; P63786: clpP; NbExp=6; IntAct=EBI-5260070, EBI-5260070;
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; BA000033; BAB94595.1; -; Genomic_DNA.
DR RefSeq; WP_001049165.1; NC_003923.1.
DR PDB; 3ST9; X-ray; 2.43 A; A/B/C/D/E/F/G=1-195.
DR PDB; 3STA; X-ray; 2.28 A; A/B/C/E/F/G/I/K/L/M/N/S/T/V=1-195.
DR PDB; 4EMM; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/V=1-195.
DR PDB; 4EMP; X-ray; 2.70 A; A/B/C/E/F/G/I/K/L/M/N/S/T/V=1-195.
DR PDBsum; 3ST9; -.
DR PDBsum; 3STA; -.
DR PDBsum; 4EMM; -.
DR PDBsum; 4EMP; -.
DR AlphaFoldDB; P63786; -.
DR SMR; P63786; -.
DR MEROPS; S14.001; -.
DR EnsemblBacteria; BAB94595; BAB94595; BAB94595.
DR GeneID; 66839059; -.
DR KEGG; sam:MW0730; -.
DR HOGENOM; CLU_058707_3_2_9; -.
DR OMA; GFKRQDP; -.
DR BRENDA; 3.4.21.92; 3352.
DR EvolutionaryTrace; P63786; -.
DR PHI-base; PHI:3005; -.
DR Proteomes; UP000000418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Protease; Serine protease.
FT CHAIN 1..195
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179654"
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:3STA"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3STA"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:3STA"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3STA"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3STA"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:3STA"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3STA"
FT HELIX 133..158
FT /evidence="ECO:0007829|PDB:3STA"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3STA"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:3STA"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3STA"
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
