ID A0A2I0FR47_9GAMM Unreviewed; 857 AA.
AC A0A2I0FR47;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=CIG19_19575 {ECO:0000313|EMBL:PKH19816.1};
OS Enterobacterales bacterium CwR94.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales.
OX NCBI_TaxID=2025587 {ECO:0000313|EMBL:PKH19816.1, ECO:0000313|Proteomes:UP000237543};
RN [1] {ECO:0000313|EMBL:PKH19816.1, ECO:0000313|Proteomes:UP000237543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CwR94 {ECO:0000313|EMBL:PKH19816.1,
RC ECO:0000313|Proteomes:UP000237543};
RA de Groot N.N.;
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. {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}.
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:PKH19816.1}.
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DR EMBL; NVXY01000017; PKH19816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0FR47; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000237543; 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 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:UP000237543};
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 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 857 AA; 95302 MW; 79C7F7F97456D813 CRC64;
MRLDRLTNKF QLALADAQSL ALGRDNQFIE PLHLMSALLS QEGGSVRPLL TTAGVDVATL
RSGIEQAISR LPQVEGTEGD VQPSADLVRV LNLCDKLAQK RGDNFISSEL FVLAALDSRG
SLNDLLKSAG ATTEKLSKAI EQMRGGESVN DQGAEDQRQA LKKYTIDLTE RAELGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL
DMGALVAGAK YRGEFEERLK GVLNDLSKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PTVEDTIAIL RGLKERYELH
HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRLQIDSKPE PLDRLERRII
QLKLEQQALK KESDDASLKR LEMLEDELSQ KERDYSELEE EWKAEKASLS GTQTVKAELE
QAKLSMEQAR RTGDLAQMSE LQYGKIPELE KQLAAATQAE GKTMRLLRNR VTDVEIADVL
ARWTGIPVAR MMEGERDKLL RMESELHQRV IGQDEAVEAV SNAIRRSRAG LSDPNRPIGS
FLFLGPTGVG KTELCKALAN FMFDSDDAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSDLIQERFG DLNYDDMKSL VMGVVGQHFR PEFINRIDEL VVFHPLGETH IASIAKIQLQ
RLYDRLAERG FELHINDDAL QLLAQTGYDP VYGARPLKRA IQQEIENPLA HQILSGGFIP
GKRIVMDVKE GHIVAHQ
//