ID A0A5B8SQ43_9GAMM Unreviewed; 866 AA.
AC A0A5B8SQ43;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-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:QEA38846.1};
GN ORFNames=FGL86_06990 {ECO:0000313|EMBL:QEA38846.1};
OS Pistricoccus aurantiacus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Pistricoccus.
OX NCBI_TaxID=1883414 {ECO:0000313|EMBL:QEA38846.1, ECO:0000313|Proteomes:UP000321272};
RN [1] {ECO:0000313|EMBL:QEA38846.1, ECO:0000313|Proteomes:UP000321272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA4606 {ECO:0000313|EMBL:QEA38846.1,
RC ECO:0000313|Proteomes:UP000321272};
RA Lee S., Ahn S., Roh S.;
RT "Genome analyses of bacteria isolated from kimchi.";
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}.
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DR EMBL; CP042382; QEA38846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B8SQ43; -.
DR KEGG; paur:FGL86_06990; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000321272; 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:UP000321272};
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 866 AA; 96053 MW; C4C0B295540AF038 CRC64;
MRFDKFTGKL QGAIADAQSL AVGQGHNQLD PGHLLMALLD NRDSGIRGLV EKAGGDAGRL
RNGLSQYLDN LPVVSQFDGE VQPSRDLARL FNLADREAQK RGDQFIASEL VLLAALEMNH
AVTRVLTQAG LNRKAVETAI DSLRGGQKVD DPNAEDNREA LEKYTLDLTA RAAEGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA NRIIDGEVPE GLKDKRVLSL
DMGALLAGAK FRGEFEERLK SVLNELAQEE GRVILFIDEL HTMVGAGKAE GSMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PNEEDTIAIL RGLKERYEVH
HRLNITDSAI IAAAKLSARY ITDRKLPDKA IDLIDEASSR IRMELDSMPE EMDRLDRRLI
QLKMEREALK KETDEASRKR LDALEAEIDE LSREYADLEE VWKSEKASIE GAAQFKAELD
KARVELDAAK RQGDLGRMSE LQYGVIPELE RKIAESEASE ASGTVQHKLL RSSVTEEEVA
EVVSRWTGIP VSKMLEGERD KLLRMEEALH ERVIGQHEAV SAVANAVRRS RAGLADPNRP
SGSFLFLGPT GVGKTELCKA LANFLFDTEE AMVRVDMSEF MEKHSVARLI GAPPGYVGYE
EGGYLTEAVR RKPYSVLLLD EVEKAHADVF NILLQVLEDG RLTDGQGRTV NFRNTVIVMT
SNLGSDIIQR MGAETESDAE QSYARMKEMV MAVVGDHFRP ELINRIDEVV VFHALGQEQI
QAIAGIQLER LRERLAEHEL ALEISDDAMA QLAVVGFDPV YGARPLKRAI QSRIENPLAQ
DLLAGKFLPG DTIHVTTKDG HLKFSK
//