ID W9TCG3_9PSED Unreviewed; 854 AA.
AC W9TCG3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:EXF45111.1};
GN ORFNames=BAY1663_02419 {ECO:0000313|EMBL:EXF45111.1};
OS Pseudomonas sp. BAY1663.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF45111.1, ECO:0000313|Proteomes:UP000019475};
RN [1] {ECO:0000313|EMBL:EXF45111.1, ECO:0000313|Proteomes:UP000019475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAY1663 {ECO:0000313|EMBL:EXF45111.1,
RC ECO:0000313|Proteomes:UP000019475};
RA Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT "Genome sequencing of Pseudomonas sp. BAY1663.";
RL Submitted (DEC-2013) 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:EXF45111.1}.
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DR EMBL; AZSV01000030; EXF45111.1; -; Genomic_DNA.
DR RefSeq; WP_037040430.1; NZ_AZSV01000030.1.
DR AlphaFoldDB; W9TCG3; -.
DR STRING; 1439940.BAY1663_02419; -.
DR PATRIC; fig|1439940.3.peg.2381; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000019475; 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, 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:UP000019475};
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; 95003 MW; 6068A265377FBBCD CRC64;
MRIDRLTSKL QLALSDAQSI AVGLDHPSIE PLHLMQALLE QQGGSIKPLL MQVGFDINAL
RQALTKELDQ LPKLQNPTGD MNLSQDLARL LNQADRLAQQ KGDQYISSEL VLLAALDGNT
RLGKLLLAQG VSKKALENAI ANLRGGEAVN DPNAEESRQA LDKYTVDMTK RAEDGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPD GLKDKRLLAL
DMGALIAGAK FRGEFEERLK AVLNELSKQE GRIILFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PSEEDTIAIL RGLKERYEVH
HGVTITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE ELDRLDRRLI
QLKIEREALK KEDDEATKKR LAKLEGDIAK LEKEYADLEE IWKSEKAEVQ GSAQIQQKIE
QAKADLEAAR RKGDLARMAE LQYGIIPDLE RSLQMVDQHG KAENQLLRNK VTDEEIAEVV
SKWTGIPVSK MLEGEREKLL RMEDMLHQRV IGQHEAVVAV ANAVRRSRAG LADPNRPSGS
FLFLGPTGVG KTELCKALAE FLFDTEEAMI RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRKP YSVVLLDEVE KAHPDVFNIL LQVLEDGRLT DSHGRTVDFR NTVVVMTSNL
GSAQIQELVG DPEAQRAAVM DAVSHHFRPE FINRIDEVVV FDPLGHEQIA GIAEIQLGRL
RKRLAERELG LELTQEAMDK LIAVGYDPVY GARPLKRAIQ RWIENPLAQQ ILSGQFAPGS
TVKARVEGEQ IVFD
//
