ID Q2FZS8_STAA8 Unreviewed; 869 AA.
AC Q2FZS8;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=SAOUHSC_00912 {ECO:0000313|EMBL:ABD30037.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD30037.1, ECO:0000313|Proteomes:UP000008816};
RN [1] {ECO:0000313|Proteomes:UP000008816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000313|Proteomes:UP000008816};
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 D.C
RL (2006).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000253; ABD30037.1; -; Genomic_DNA.
DR RefSeq; WP_000353970.1; NZ_LS483365.1.
DR RefSeq; YP_499465.1; NC_007795.1.
DR AlphaFoldDB; Q2FZS8; -.
DR SMR; Q2FZS8; -.
DR STRING; 93061.SAOUHSC_00912; -.
DR PaxDb; 1280-SAXN108_0969; -.
DR GeneID; 3920799; -.
DR KEGG; sao:SAOUHSC_00912; -.
DR PATRIC; fig|93061.5.peg.833; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OMA; GPEHILM; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Hydrolase {ECO:0000313|EMBL:ABD30037.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABD30037.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008816};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 50..106
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 411..525
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 98331 MW; 9CC9FA8948FC060D CRC64;
MDINKMTYAV QSALQQAVEL SQQHKLQNIE IEAILSAALN ESESLYKSIL ERVNIEVDQL
NKAYEDKLNT YASVEGDNIQ YGQYISQQAN QLITKAESYM KEYEDEYISM EHILRSAMDI
DQTTKHYINN KVEVIKEIIK KVRGGNHVTS QNPEVNYEAL AKYGRDLVEE VRQGKMDPVI
GRDEEIRNTI RILSRKTKNN PVLIGEPGVG KTAIVEGLAQ RIVKKDVPES LLDKTVFELD
LSALVAGAKY RGEFEERLKA VLKEVKESDG RIILFIDEIH MLVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLNEYRE YIEKDSALER RFQKVAVSEP DVEDTISILR GLKERYEVYH
GVRIQDRALV AAAELSDRYI TDRFLPDKAI DLVDQACATI RTEMGSNPTE LDQVNRRVMQ
LEIEESALKN ESDNASKQRL QELQEELANE KEKQAALQSR VESEKEKIAN LQEKRAQLDE
SRQALEDAQT NNNLEKAAEL QYGTIPQLEK ELRELEDNFQ DEQGEDTDRM IREVVTDEEI
GDIVSQWTGI PVSKLVETER EKLLHLSDIL HKRVVGQDKA VDLVSDAVVR ARAGIKDPNR
PIGSFLFLGP TGVGKTELAK SLAASLFDSE KHMIRIDMSE YMEKHAVSRL IGAPPGYIGH
DEGGQLTEAV RRNPYSVILL DEVEKAHTDV FNVLLQILDE GRLTDSKGRS VDFKNTIIIM
TSNIGSQVLL ENVKETGEIT ESTEKAVMTS LNAYFKPEIL NRMDDIVLFK PLSIDDMSMI
VDKILTQLNI RLLEQRISIE VSDDAKAWLG QEAYEPQYGA RPLKRFVQRQ IETPLARMMI
KEGFPEGTTI KVNLNSDNNL TFNVEKIHE
//