ID A0A545T1U8_9GAMM Unreviewed; 878 AA.
AC A0A545T1U8;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TQV71207.1};
GN ORFNames=FKG94_20195 {ECO:0000313|EMBL:TQV71207.1};
OS Exilibacterium tricleocarpae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Exilibacterium.
OX NCBI_TaxID=2591008 {ECO:0000313|EMBL:TQV71207.1, ECO:0000313|Proteomes:UP000319732};
RN [1] {ECO:0000313|EMBL:TQV71207.1, ECO:0000313|Proteomes:UP000319732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R142 {ECO:0000313|EMBL:TQV71207.1,
RC ECO:0000313|Proteomes:UP000319732};
RA Wang G.;
RT "Whole genome sequence for Cellvibrionaceae sp. R142.";
RL Submitted (JUN-2019) 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:TQV71207.1}.
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DR EMBL; VHSG01000022; TQV71207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A545T1U8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000319732; 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:UP000319732};
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 878 AA; 97571 MW; 0066D9A5E8DD185D CRC64;
MRIDRLTNQL QIALSDAQSL AVGRDHNQLE PVHVLLAMLD QQGGTVRPLL AQAGFDVTGL
RNELAKQLDN LARVQSPTGD VHMSAETGRL LNLADKRAQE VGDKFISSES LLLAAMHDGN
SALGKLLNQF GDKQRLESAV DKVRGGETVD DPDAEGNRQA LEKYTIDLTA RAEAGKLDPV
IGRDDEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNKQLLSL
DLGSLLAGAK FRGEFEERLK AVLNELSKQE GRIILFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR KFIEKDAALE RRFQKVLVDE PSEEDTIAIL RGLKERYEVH
HGVDITDSAI IAAAKLSQRY ITDRQLPDKA IDLVDEAASR IRMEIDSKPE EMDRLERRLI
QLKIEREAVK KDTSESAKKQ LQLLDDDIEQ AERKFADLEE IWRAEKAALH GSHEIKSNLE
QVRLDLEAAR RAGDLARMSE LQYGVIPELE KQLDMASQAE MMEMKLLRNK VTDEEIAEVV
SKWTGIPVAK MLEGEREKLL RMEDALHRRV IGQQEAVVAV SNAVRRSRAG LADPNRPNGS
FLFLGPTGVG KTELCKALAE FLFDSEDAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRKP YSVLLLDEVE KAHADVFNIL LQVLEDGRLT DGQGRTVDFR NTVVVMTSNL
GSDRIQELAQ DRSFDTISFD SDENSDTAAN EHRRAAIKEA VMEVVASHFR PEFVNRIDEL
VVFDPLGQAQ IRGIATIQLD LLRRRLAERE LKLELDDAVM DKLVQVGFDP VYGARPLKRA
IQQQIENPLA QDVLAGKFAP GATVVGRLDE RGQLVFTG
//