ID C3KE86_PSEFS Unreviewed; 854 AA.
AC C3KE86;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB1 {ECO:0000313|EMBL:CAY47051.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=PFLU_0782 {ECO:0000313|EMBL:CAY47051.1};
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY47051.1};
RN [1] {ECO:0000313|EMBL:CAY47051.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY47051.1};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
RN [2] {ECO:0000313|EMBL:CAI2795091.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAI2795091.1};
RA Fortmann-Grote C.;
RL Submitted (OCT-2023) 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; OV986001; CAI2795091.1; -; Genomic_DNA.
DR EMBL; AM181176; CAY47051.1; -; Genomic_DNA.
DR RefSeq; WP_012722152.1; NC_012660.1.
DR AlphaFoldDB; C3KE86; -.
DR STRING; 294.SRM1_04885; -.
DR PATRIC; fig|216595.4.peg.1019; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP001152918; 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 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, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
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 854 AA; 95352 MW; 0ACBF4B4128F1793 CRC64;
MRIDRLTSKL QLALSDSQSL AVGLDHPAIE PAHLMQALLE QQGGSIKPLL MQVGFDVNSL
RKELSKELDQ LPKIQNPTGD VNMSQDLARL LNQADRLAQQ KGDQFISSEL VLLAAMDENS
KLGKLLLGQG VSKKALENAI NNLRGGDAVN DPNHEESRQA LDKYTVDLTK RAEEGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINGEVPD GLKGKRLLSL
DMGSLIAGAK FRGEFEERLK SLLNELSKQE GQIILFIDEL HTMVGAGKGE GSMDAGNMLK
PALARGELHC VGATTLNEYR QYIEKDAALE RRFQKVLVEE PSEEDTIAIL RGLKERYEVH
HKVAITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE VLDRLDRRLI
QLKVESQALK KEEDDAAKKR LEKLQEEIVR LEREYSDLEE IWTSEKAEVQ GSAQIQQKIE
QSRQELEAAR RKGDLNRMAE LQYGVIPDLE RSLQMVDQHG KSENQLLRSK VTEEEIAEVV
SKWTGIPVSK MLEGERDKLL KMESLLHQRV IGQEEAVVAV SNAVRRSRAG LSDPNRPSGS
FMFLGPTGVG KTELCKALAE FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLEDGRLT DSHGRTVDFR NTVIVMTSNL
GSAQIQELVG DREAQRAAVM DALTTHFRPE FINRVDEVVI FEPLARDQIA GITEIQLGRL
RGRLTERELS LDLSQEALDK LIAVGYDPVY GARPLKRAIQ RWIENPLAQL ILSGSFMPGT
SVTATVENDE IVFH
//
