ID   CLPC_STAEQ              Reviewed;         817 AA.
AC   Q5HRM8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC;
GN   Name=clpC; OrderedLocusNames=SERP0165;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53548.1; -; Genomic_DNA.
DR   RefSeq; WP_002445729.1; NC_002976.3.
DR   AlphaFoldDB; Q5HRM8; -.
DR   SMR; Q5HRM8; -.
DR   STRING; 176279.SERP0165; -.
DR   EnsemblBacteria; AAW53548; AAW53548; SERP0165.
DR   KEGG; ser:SERP0165; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Repeat;
KW   Stress response.
FT   CHAIN           1..817
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpC"
FT                   /id="PRO_0000269688"
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   817 AA;  91012 MW;  76E6455923462294 CRC64;
     MLFGRLTERA QRVLAHAQEE AIRLNHSNIG TEHLLLGLMK EPEGIAAKVL VSFNITEDKV
     IEEVEKLIGH GQEQMGTLHY TPRAKKVIEL SMDEARKLHH NFVGTEHILL GLIRENEGVA
     ARVFANLDLN ITKARAQVVK ALGSPEMSNK NAQANKSNNT PTLDGLARDL TVIAKDGTLD
     PVVGRDKEIT RVIEVLSRRT KNNPVLIGEP GVGKTAIAEG LAQAIVKNEV PETLKDKRVM
     SLDMGTVVAG TKYRGEFEER LKKVMEEIHQ AGNVILFIDE LHTLVGAGGA EGAIDASNIL
     KPALARGELQ CIGATTLDEY RKNIEKDAAL ERRFQPIQVD EPTVEDTIEI LKGLRDRYEA
     HHRINISDEA LEAAAKLSDR YVSDRFLPDK AIDLIDEASS KVRLKSHTTP SNLKEIEQEI
     DKVKNEKDAA VHAQEFENAA NLRDKQSKLE KQYEDAKNEW KNAQGGLDTA LSEENIAEVI
     AGWTGIPLTK INETESDRLL NLEDTLHKRV IGQNDAVNSI SKAVRRARAG LKDPKRPIGS
     FIFLGPTGVG KTELARALAE SMFGEDDAMI RVDMSEFMEK HAVSRLVGAP PGYVGHDDGG
     QLTEKVRRKP YSVILFDEIE KAHPDVFNIL LQVLDDGHLT DTKGRTVDFR NTVIIMTSNV
     GAQELQDQRF AGFGGASEGS DYETVRKTMM KELKNSFRPE FLNRVDDIIV FHKLTKDELK
     EIVTMMVNKL THRLSEQNIN IVVTDKAKEK IAEEGYDPEY GARPLIRAIQ KTVEDNLSEL
     ILDGNKIEGK EVTIDHDGKE FKYDIYEITA KKETTES