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Database: UniProt
Entry: A0A0F5V740_9GAMM
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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
//
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