ID   CLPC_STAS1              Reviewed;         820 AA.
AC   Q49V34;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC;
GN   Name=clpC; OrderedLocusNames=SSP2231;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE19376.1; -; Genomic_DNA.
DR   RefSeq; WP_011303851.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49V34; -.
DR   SMR; Q49V34; -.
DR   STRING; 342451.SSP2231; -.
DR   PRIDE; Q49V34; -.
DR   EnsemblBacteria; BAE19376; BAE19376; SSP2231.
DR   KEGG; ssp:SSP2231; -.
DR   PATRIC; fig|342451.11.peg.2222; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000006371; 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..820
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpC"
FT                   /id="PRO_0000269691"
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   820 AA;  91435 MW;  8DB843D4C8D6AE88 CRC64;
     MLFGRLTERA QRVLAHAQEE AIRLNHSNIG TEHLLLGLMK EPEGIAAKVL ETFEITEEKV
     VEEVEKLIGH GQEQMGALHY TPRAKKVIEL SMDEARKLHH NFVGTEHILL GLIRENEGVA
     ARVFANLDLN ITKARAQVVK ALGSPEMSNK NAQANKSNNT PTLDSLARDL TVIAKDGTLD
     PVIGRDKEIT RVIEVLSRRT KNNPVLIGEP GVGKTAIAEG LAQAIVNNEV PETLKGKRVM
     SLDMGTVVAG TKYRGEFEER LKKVMEEIHQ AGNVILFIDE LHTLVGAGGA EGAIDASNIL
     KPALARGELQ CIGATTLDEY RKNIEKDAAL ERRFQPVQVD EPTVEDTIEI LKGLRDRYEA
     HHRINISDEA LVSAAKLSHR YVSDRFLPDK AIDLIDEASS KVRLKSHTTP PNLKEIEQQI
     EQVKNEKDAA VHAQEFENAA NLRDKQTKLE KQYEEANTNW KNTQNGDNTS LSEEDIGEVI
     AGWTGIPLTK INETESDRLL NLEDTLHNRV IGQKDAVTSI SKAVRRARAG LKDPKRPIGS
     FIFLGPTGVG KTELARALAE SMFGEDDAMI RVDMSEFMEK HAVSRLVGAP PGYVGHDDGG
     QLTEKVRRKP YSVILFDEIE KAHPDVFNIL LQVLDDGHLT DTKGRRVDFR NTVIIMTSNV
     GAQELQDQRF AGFGGATEGQ DYESIRKTMM KELKNAFRPE FLNRVDDIIV FHKLSKDELK
     QIVTMMVNKL TNRLSEQDIN ISVTEAAKEK IAEEGYDPEY GARPLIRAIQ KTVEDNLSEL
     ILDGNQIEGK EVKIDHDGKE FKYDITERQD SAKDKETSES