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Database: UniProt
Entry: CLPC_STAHJ
LinkDB: CLPC_STAHJ
Original site: CLPC_STAHJ 
ID   CLPC_STAHJ              Reviewed;         824 AA.
AC   Q4L3I4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC;
GN   Name=clpC; OrderedLocusNames=SH2484;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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; AP006716; BAE05793.1; -; Genomic_DNA.
DR   RefSeq; WP_011276736.1; NC_007168.1.
DR   AlphaFoldDB; Q4L3I4; -.
DR   SMR; Q4L3I4; -.
DR   KEGG; sha:SH2484; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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..824
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpC"
FT                   /id="PRO_0000269690"
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   824 AA;  91612 MW;  49FF2DFB72777CF5 CRC64;
     MLFGRLTERA QRVLAHAQEE AIRLNHSNIG TEHLLLGLMK EPEGIAAKVL ESFNITEDKV
     IEEVEKLIGH GQDQTGTLHY TPRAKKVIEL SMDEARKLHH NFVGTEHILL GLIRENEGVA
     ARVFANLDLN ITKARAQVVK ALGSPEMSNK NATANKSNNT PTLDGLARDL TVIAKDGTLD
     PVVGRDKEIT RVIEVLSRRT KNNPVLIGEP GVGKTAIAEG LAQAIVNNEV PETLKGKRVM
     SLDMGTVVAG TKYRGEFEER LKKVMEEIHQ AGNVILFIDE LHTLVGAGGA EGAIDASNIL
     KPALARGELQ CIGATTLDEY RKNIEKDAAL ERRFQPIQVD EPTVEDTIAI LKGLRDRYEA
     HHRINISDEA LEAAAKLSDC YVSDRFLPDK AIDLIDEASS KVRLKSHTTP NNLKEIEQEI
     EKVKNEKDAA VHAQEFENAA NLRDKQTKLE KQYEDAKNEW KTTQGDQSTS LSKEDIGEVI
     AGWTGIPLTK INETESDRLL NLEQTLHDRV IGQNDAVTSI SKAVRRARAG LKDPKRPIGS
     FIFLGPTGVG KTELARALAE SMFGEEDAMI RVDMSEFMEK HAVSRLVGAP PGYVGHDEGG
     QLTEKVRRKP YSVILFDEIE KAHPDVFNIL LQVLDDGHLT DTKGRQVDFR NTVIIMTSNV
     GAQELQDQRF AGFGGGSEGH DYETIRKTMM KELKNSFRPE FLNRVDDIIV FHKLSKDELK
     EIVTMMVNKL TQRLSEQDIN IVVTDKAKEK IAEEGYDPEY GARPLIRAIQ KTVEDNLSEL
     ILDGNQIEGK EVVIDHDGDE FKYNINEKNN GISDEGNEVT ETEA
//
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