ID A0A1P8UHY0_9GAMM Unreviewed; 863 AA.
AC A0A1P8UHY0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BW247_10125 {ECO:0000313|EMBL:APZ43404.1};
OS Acidihalobacter ferrooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Acidihalobacter.
OX NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ43404.1, ECO:0000313|Proteomes:UP000243807};
RN [1] {ECO:0000313|EMBL:APZ43404.1, ECO:0000313|Proteomes:UP000243807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V8 {ECO:0000313|EMBL:APZ43404.1,
RC ECO:0000313|Proteomes:UP000243807};
RA Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA Watkin E.L.J.;
RT "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT V8).";
RL Submitted (JAN-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. {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; CP019434; APZ43404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8UHY0; -.
DR STRING; 1765967.BW247_10125; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000243807; Chromosome.
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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000243807};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 95713 MW; 8CB3CE6036DCC43C CRC64;
MRMDKLTSKF QMALADAQSL AVGRDHQFIE PLHLMRALLD QEGGTVRPLL TKAGVNVNQL
RARLDEALDS LPSVEGTGGD VHVSNELGNL LNLTDKLAQK RQDAYISSEL FLLAVLDGKG
HLHDLLTQAG GVRGAIEKAI DEMRGGATVD DPNAEDSRKA LEKYTIDLTE RAEQGKLDPV
IGRDEEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVDGAVPE GLKSKRVLSL
DLGALLAGAK FRGDFEERLK AVLNDLSKQE GRIILFIDEI HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEMDAALE RRFQKVLVDE PSVEDTIAIL RGLKERYEVH
HGVEITDPAI VAAAMLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE EMDRLERRLI
QLKIEREALK KESDEASKKR LADLEEQIAK LEREFSDLDE IWKSEKAAVQ GATHIKEELE
RVRTELETAR RAGDLGRMSE LQYGRIPELE RQLAMASQAE MQEMTLLRNK VSDEEIAEVV
SRWTGIPVSK MLEGEKEKLL RMEDVLGQRV VGQNEAVKAV ANAIRRSRAG LSDPNRPNGS
FLFLGPTGVG KTELTKSLAS FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRKP YSVILLDEVE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
GSQTIQELAG EENYEAMKAA VMEVVGGHFR PEFINRIDEV VVFHPLGREQ IRAITRIQLD
YLRRRLADRD MGLEISDAAL DRLGEAGFDP VYGARPLKRA IQQDVENPLA QAILGGEFLP
GDVIYVDAGE TGLNFSTIAT DAA
//