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Database: UniProt
Entry: A0A3N9TFQ9_9VIBR
LinkDB: A0A3N9TFQ9_9VIBR
Original site: A0A3N9TFQ9_9VIBR 
ID   A0A3N9TFQ9_9VIBR        Unreviewed;       857 AA.
AC   A0A3N9TFQ9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
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:RQW63087.1};
GN   ORFNames=EES38_12320 {ECO:0000313|EMBL:RQW63087.1};
OS   Vibrio viridaestus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2487322 {ECO:0000313|EMBL:RQW63087.1, ECO:0000313|Proteomes:UP000281112};
RN   [1] {ECO:0000313|EMBL:RQW63087.1, ECO:0000313|Proteomes:UP000281112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LJC006 {ECO:0000313|EMBL:RQW63087.1,
RC   ECO:0000313|Proteomes:UP000281112};
RA   Liang J.;
RT   "Vibrio LJC006 sp. nov., isolated from seawater during the bloom of the
RT   enteromorpha.";
RL   Submitted (NOV-2018) 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:RQW63087.1}.
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DR   EMBL; RJVQ01000004; RQW63087.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N9TFQ9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000281112; 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:UP000281112};
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          405..461
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   857 AA;  96098 MW;  5DFC1FF9CA2A3B1F CRC64;
     MRLDRFTSKF QVAISDAQSL ALGRDHQYIE PVHLMVALMD QDGSPIRPLL TMMNVDAMQL
     RSKLGEELDR LPKVTGIGAD VQLSSGLGYL FNMCDKIAQK RQDAYISSEI FLLAAIQDKG
     PLGQLCKDLG VTEKKVTDAI EKVRGGQKVK DQNAEDLRQA LEKFTVDLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINNEVPE GLRGRRVLSL
     DMGALVAGAK YRGEFEERLK SVLNELAKEE GNVILFIDEL HTMVGAGKGE GSMDAGNMLK
     PALARGELHC VGATTLDEYR QYVEKDPALE RRFQKVLVDE PSVEDTVAIL RGLKERYELH
     HHVEITDPAI VAAATLSHRY VSDRQLPDKA IDLIDEAASS IRLQIDSKPE ELDKLERRII
     QLKIEQQALS NEHDNASNKR LEILNEELTE REKEYAELEE VWNAEKAALS GTQHIKSELE
     QARMDMDVAR RAGDLNRMSE LQYGRIPELE KQLDLAAQAE MQEMTLLRNK VTDAEIAEVL
     SKQTGIPVSK MLEAEKEKLL QMESVLHKRV IGQVEAVDVV SNAIRRSRAG LSDPNRPIGS
     FLFLGPTGVG KTELCKTLAN FMFDSEEAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
     GSSQIQEGFK DLNYEQMKAQ VMDVVAHHFR PEFLNRVDES VVFHPLGREQ IKSIASIQIE
     RLRQRMHERD YELDMDEKAL DLIAQVGFDP VYGARPLKRA IQQEVENPLA KAMLSGEFTP
     GRPIKLTAVD GKILATQ
//
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