ID A0A2K4C454_9STAP Unreviewed; 870 AA.
AC A0A2K4C454;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PNZ68904.1};
GN ORFNames=CD158_02340 {ECO:0000313|EMBL:PNZ68904.1};
OS Staphylococcus auricularis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=29379 {ECO:0000313|EMBL:PNZ68904.1, ECO:0000313|Proteomes:UP000242470};
RN [1] {ECO:0000313|EMBL:PNZ68904.1, ECO:0000313|Proteomes:UP000242470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12101 {ECO:0000313|EMBL:PNZ68904.1,
RC ECO:0000313|Proteomes:UP000242470};
RA Cole K., Golubchik T., Russell J., Foster D., Llewelyn M., Wilson D.,
RA Crook D., Paul J.;
RT "Draft genome sequences of 64 type strains of genus Staph aureus.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNZ68904.1}.
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DR EMBL; PPQW01000008; PNZ68904.1; -; Genomic_DNA.
DR RefSeq; WP_059106454.1; NZ_QVVG01000016.1.
DR STRING; 29379.GCA_001500315_00946; -.
DR GeneID; 64982663; -.
DR KEGG; saul:I6G39_08365; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000242470; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
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 78, MITOCHONDRIAL; 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};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000242470};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000256|RuleBase:RU362034}.
SQ SEQUENCE 870 AA; 98428 MW; BDE5655FE480815D CRC64;
MDVNQMTYKV QESLQKAIGL AQTYENQNIE IEAVLKAALE ENESLFNSIL ERANIDTEAL
GQSYTNKLKN YPNVQGDNVQ YGQYISPKTN ELFNKAESYM SSYEDEYISM EHLLLAANDI
DDTTKQYIGN KIEVVKEIIN KVRGGNHVTS QNPEVNYEAL EKYGRDLVEE VRQGNMDPVI
GRDEEIRNAI RILSRKTKNN PVLIGEPGVG KTAIVEGLAQ RIVRKDVPES LLDKTIFELD
LSAMVAGAKY RGEFEERLKA VLKEVKESDG RIILFIDEIH MLVGAGKTEG SMDAGNMLKP
MLARGELHCI GATTLNEYRE NIEKDSALER RFQKVQVSEP NVEDTISILR GLKERYEVYH
GVRIQDRALV AAAELSDRYI TDRFLPDKAI DLVDQACATI RTEMGSNPTE LDQVNRRVMQ
LEIEESALKN ESDNASKQRL QELQEELSNE KEKQAEIQSR VDQEKDKISA LQDKRTELDE
SRKALEDAEN NYDLEKAAEL QHGKIPQLEK ELRELEDAFQ DEQPDGQDRI IREVVSDEEI
GDIVSSWTGI PVSKLVETER EKLLNLSDIL HERVVGQDKA VDLVSDAVVR ARAGIKDPNR
PIGSFLFLGP TGIGKTELAK SLASTLFDSE KHMIRIDMSE YMEKHSVSRL IGAPPGYVGH
DEGGQLTEAV RRNPYSVILL DEIEKAHTDV FNVLLQILDE GRLTDSQGRS VDFKNTIIIM
TSNIGSQILL ENVKDSGVIT ENTEQAVMAN VNEYFKPEIL NRMDDIVLFK PLTVDDMSLI
VDKVVTQLNI RLMDQRISID VSDKAKKWLG EEAYEPQFGA RPLKRFVQRQ IETPLARRMI
REDMPEGTTV KIDLTDDGLT FDQIEPETVQ
//
