CLPC_STAA8
ID CLPC_STAA8 Reviewed; 818 AA.
AC Q2G0P5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC;
GN Name=clpC; OrderedLocusNames=SAOUHSC_00505;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, INDUCTION, AND SUBUNIT.
RX PubMed=15554981; DOI=10.1111/j.1365-2958.2004.04368.x;
RA Frees D., Chastanet A., Qazi S., Soerensen K., Hill P., Msadek T.,
RA Ingmer H.;
RT "Clp ATPases are required for stress tolerance, intracellular replication
RT and biofilm formation in Staphylococcus aureus.";
RL Mol. Microbiol. 54:1445-1462(2004).
RN [3]
RP INDUCTION.
RC STRAIN=SH1000;
RX PubMed=22126623; DOI=10.1111/j.1574-6968.2011.02468.x;
RA Sitthisak S., Kitti T., Boonyonying K., Wozniak D., Mongkolsuk S.,
RA Jayaswal R.K.;
RT "McsA and the roles of metal-binding motif in Staphylococcus aureus.";
RL FEMS Microbiol. Lett. 327:126-133(2012).
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. Required for biofilm formation. May act as a
CC chaperone regulating CtsR activity. {ECO:0000269|PubMed:15554981}.
CC -!- SUBUNIT: May interact with ClpP. {ECO:0000269|PubMed:15554981}.
CC -!- INDUCTION: By heat shock. Transcriptionally regulated by CtsR
CC (PubMed:15554981). Up-regulated by heavy metals such as Cu(2+) and
CC Cd(2+), but Zn(2+) and Co(2+) have no effect (PubMed:22126623). Forms
CC part of an operon with ctsR, mcsA and mcsB.
CC {ECO:0000269|PubMed:15554981, ECO:0000269|PubMed:22126623}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD29654.1; -; Genomic_DNA.
DR RefSeq; WP_000897132.1; NZ_LS483365.1.
DR RefSeq; YP_499078.1; NC_007795.1.
DR PDB; 6EM8; EM; 8.40 A; A/B/C/D/E/F/G/H/I/L=1-818.
DR PDBsum; 6EM8; -.
DR AlphaFoldDB; Q2G0P5; -.
DR SMR; Q2G0P5; -.
DR STRING; 1280.SAXN108_0578; -.
DR EnsemblBacteria; ABD29654; ABD29654; SAOUHSC_00505.
DR GeneID; 3920417; -.
DR KEGG; sao:SAOUHSC_00505; -.
DR PATRIC; fig|93061.5.peg.452; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR OMA; SKMMQGE; -.
DR PRO; PR:Q2G0P5; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:1990170; P:stress response to cadmium ion; IDA:UniProtKB.
DR GO; GO:1990169; P:stress response to copper ion; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response; Virulence.
FT CHAIN 1..818
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpC"
FT /id="PRO_0000269679"
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
