ID   CLPC_STAAR              Reviewed;         818 AA.
AC   Q6GJE4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC;
GN   Name=clpC; OrderedLocusNames=SAR0528;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Required for growth at high temperatures, probably by acting
CC       as a chaperone during heat shock and targeting heat-denatured proteins
CC       for degradation by ClpP. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX571856; CAG39550.1; -; Genomic_DNA.
DR   RefSeq; WP_000897132.1; NC_002952.2.
DR   AlphaFoldDB; Q6GJE4; -.
DR   SMR; Q6GJE4; -.
DR   KEGG; sar:SAR0528; -.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Repeat; Stress response.
FT   CHAIN           1..818
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpC"
FT                   /id="PRO_0000269685"
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   DOMAIN          417..452
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   REGION          6..71
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          80..144
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          163..410
FT                   /note="I"
FT   REGION          471..662
FT                   /note="II"
FT   BINDING         208..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         545..552
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   818 AA;  91037 MW;  404DBB1643BAA31F CRC64;
     MLFGRLTERA QRVLAHAQEE AIRLNHSNIG TEHLLLGLMK EPEGIAAKVL ESFNITEDKV
     IEEVEKLIGH GQDHVGTLHY TPRAKKVIEL SMDEARKLHH NFVGTEHILL GLIRENEGVA
     ARVFANLDLN ITKARAQVVK ALGNPEMSNK NAQASKSNNT PTLDSLARDL TVIAKDGTLD
     PVIGRDKEIT RVIEVLSRRT KNNPVLIGEP GVGKTAIAEG LAQAIVNNEV PETLKDKRVM
     SLDMGTVVAG TKYRGEFEER LKKVMEEIQQ AGNVILFIDE LHTLVGAGGA EGAIDASNIL
     KPALARGELQ CIGATTLDEY RKNIEKDAAL ERRFQPVQVD EPSVVDTVAI LKGLRDRYEA
     HHRINISDEA IEAAVKLSNR YVSDRFLPDK AIDLIDEASS KVRLKSHTTP NNLKEIEQEI
     EKVKNEKDAA VHAQEFENAA NLRDKQTKLE KQYEEAKNEW KNAQNGMSTS LSEEDIAEVI
     AGWTGIPLTK INETESEKLL SLEDTLHERV IGQKDAVNSI SKAVRRARAG LKDPKRPIGS
     FIFLGPTGVG KTELARALAE SMFGDDDAMI RVDMSEFMEK HAVSRLVGAP PGYVGHDDGG
     QLTEKVRRKP YSVILFDEIE KAHPDVFNIL LQVLDDGHLT DTKGRTVDFR NTIIIMTSNV
     GAQELQDQRF AGFGGSSDGQ DYETIRKTML KELKNSFRPE FLNRVDDIIV FHKLTKEELK
     EIVTMMVNKL TNRLSEQNIN IIVTDKAKDK IAEEGYDPEY GARPLIRAIQ KTIEDNLSEL
     ILDGNQIEGK KVTVDHDGKE FKYDIAEQTS ETKTPSQA