ID A0A233HLD8_9VIBR Unreviewed; 858 AA.
AC A0A233HLD8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=B9J89_12625 {ECO:0000313|EMBL:OXX62330.1};
OS Vibrio sp. V15_P4S5T153.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1938669 {ECO:0000313|EMBL:OXX62330.1, ECO:0000313|Proteomes:UP000215241};
RN [1] {ECO:0000313|EMBL:OXX62330.1, ECO:0000313|Proteomes:UP000215241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V15_P4S5T153 {ECO:0000313|EMBL:OXX62330.1,
RC ECO:0000313|Proteomes:UP000215241};
RA Vazquez-Rosas-Landa M.;
RT "High clonality and local adaptation shapes Vibrionaceae linages within an
RT endangered oasis.";
RL Submitted (FEB-2017) 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:OXX62330.1}.
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DR EMBL; NDIJ01000015; OXX62330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A233HLD8; -.
DR Proteomes; UP000215241; 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 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..461
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 96071 MW; 3C63F435E35976E9 CRC64;
MRLDRFTSKF QIAISDAQSL ALGRDHQYIE PVHLMVALLD QNGSPIRPLL TMLSVDVMQL
RSKLSEILDR LPKVSGIGGD VQLSSAMGTM FNLCDKLAQK RQDSYISSEV FLLAALEDKG
ALGQLLKEIG LTEKKVSEAI EKVRGGQKVN DPNAEELRQA LEKFTIDLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVIIGEPGV GKTAIVEGLA QRIINNEVPE GLRGRRVLSL
DMGSLVAGAK YRGEFEERLK SVLNELAKEE GNVILFIDEL HTMVGAGRGE GAMDAGNMLK
PALARGDLHC VGATTLDEYR QYIEKDPALE RRFQKVLVDE PSVEDTVAIL RGLKERYELH
HHVEITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRMQIDSKPE SLDKLERKII
QLKIEQQALT NEHDEASEKR LQVLNEELQV KEREFAELEE VWNAEKAALS GTQHIKSELE
QARMDMDFAR RAGDLNRMSE LQYGRIPELE KQLDLATQAE MQEMTLLRNK VTDVEIAEVL
SKQTGIPVSK MLEAEKEKLL QMEDALHQRV IGQVEAVEVV SNAIRRSRAG LSDPNRPIGS
FLFLGPTGVG KTELCKTLAN FMFDSEDAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
YLTEAIRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSSQIQEKFA SLDYEGIKKE VMEIVGKHFR PEFLNRVDES VVFHPLAQEQ IKSIASIQLA
RLGKRMEEKG YQLEVSEKAL ELISQVGFDP VYGARPLKRA IQQSVENPLA KEILAGRILP
DKKVKLVVSN DQIIAHQD
//