ID A0A0F5V740_9GAMM Unreviewed; 857 AA.
AC A0A0F5V740;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=KY46_20590 {ECO:0000313|EMBL:KKC98015.1};
OS Photobacterium halotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=265726 {ECO:0000313|EMBL:KKC98015.1, ECO:0000313|Proteomes:UP000033633};
RN [1] {ECO:0000313|EMBL:KKC98015.1, ECO:0000313|Proteomes:UP000033633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MELD1 {ECO:0000313|EMBL:KKC98015.1,
RC ECO:0000313|Proteomes:UP000033633};
RA Mathew D.C., Huang C.-C.;
RT "Mercury Reductase activity and rhizosphere competence traits in the genome
RT of root associated Photobacterium halotolerans MELD1.";
RL Submitted (DEC-2014) 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:KKC98015.1}.
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DR EMBL; JWYV01000028; KKC98015.1; -; Genomic_DNA.
DR RefSeq; WP_046222469.1; NZ_JWYV01000028.1.
DR AlphaFoldDB; A0A0F5V740; -.
DR STRING; 265726.KY46_20590; -.
DR PATRIC; fig|265726.11.peg.2926; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000033633; 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:UP000033633};
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; 95548 MW; DF005B9D02F68598 CRC64;
MRLDRFTSKF QLAISDAQSL ALGRDHQYIE PVHLMMALMN QDSSTTRPLL TLLNVDITQL
RSSLSEQLDR LPKVSGIGGD VQLSHGMGVL FNMCDKLAQK RKDKYISSEL FILAAVDDKG
PLGELLRKFG LSAEKVEQAI EKIRGGQKVD DPNAEENRQA LEKFTIDLTE RAEQGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLRNKRVLSL
DMGALIAGAK YRGEFEERLK SVLNELAQEE GSVILFIDEL HTMVGAGKGE GAMDAGNMLK
PALARGELHC VGATTLDEYR QFIEKDAALE RRFQKVLVEE PNVEDTIAIL RGLKERYALH
HHVEITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRMQIDSKPE SLDRLERRII
QLKIEQQALS KENDDASQKR LAVLSEELAG KEKEYAELEE VWNAEKAALS GTQHIKAELE
QARTDMEIAR RAGDLNRMSE LQYGKIPALE KQLDLAAQAE MQEMSLLKNR VTDAEIAEVL
SRQTGIPVSR MLEGERDKLL RMEAALHQRV IGQDEAVNSV ANAIRRSRAG LSDPNRPIGS
FLFLGPTGVG KTELCKALAN FMFDSDDAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NSVIIMTSNL
GSDRIQEHFG ELDYDGIKQL VMDVVGHHFR PEFINRVDET VVFHPLGDMH IKDIARIQIG
RLSARLEEKG FELKVDESAL DLIASAGFDP VYGARPLKRA IQQYIENPLA QDILSGKLTV
DKPIVLTAKD EHISTSQ
//