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Database: UniProt
Entry: A0A0M0HWL0_9VIBR
LinkDB: A0A0M0HWL0_9VIBR
Original site: A0A0M0HWL0_9VIBR 
ID   A0A0M0HWL0_9VIBR        Unreviewed;       857 AA.
AC   A0A0M0HWL0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AKJ31_16530 {ECO:0000313|EMBL:KOO06456.1};
OS   Vibrio hepatarius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=171383 {ECO:0000313|EMBL:KOO06456.1, ECO:0000313|Proteomes:UP000037530};
RN   [1] {ECO:0000313|Proteomes:UP000037530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19134 {ECO:0000313|Proteomes:UP000037530};
RA   Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT   "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT   isolated from the Solomon Islands.";
RL   Submitted (AUG-2015) 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:KOO06456.1}.
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DR   EMBL; LHPI01000018; KOO06456.1; -; Genomic_DNA.
DR   RefSeq; WP_053410199.1; NZ_LHPI01000018.1.
DR   AlphaFoldDB; A0A0M0HWL0; -.
DR   STRING; 171383.AKJ31_16530; -.
DR   PATRIC; fig|171383.3.peg.3378; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000037530; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:KOO06456.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KOO06456.1};
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   857 AA;  95820 MW;  54E38EDC1B3F8561 CRC64;
     MRLDRFTSKF QIAISDAQSL ALGRDHQYIE PVHLMVALMD QDGSPIRPLL TMLNVDVTQL
     RSKLSEILDR LPKVSGIGGD VQLSSSMGTL FNLCDKVAQK RQDTYISSEI FLLAAIEDRG
     PLGALLKEQG LTEAKISEAI DKVRGGQKVN DPNAEELRQA LEKFTIDLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVIIGEPGV GKTAIVEGLA QRIINNEVPE GLRGRRVLAL
     DMGALVAGAK YRGEFEERLK SVLNELAKEE GNVILFIDEV HTMVGAGKGE GSMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDPALE RRFQKVLVDE PSVEDTVAIL RGLKERYELH
     HHVEITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRMQIDSKPE ALDKLERKII
     QLKIEQQALN NEHDDASEKR LNMLNEELAE KEREFAELEE VWNAEKAALS GTQHIKSELE
     QARMDMEFAR RAGDLNRMSE LQYGRIPELE KQLDLATQAE MQEMTLLRNK VTDNEIAEVL
     SKQTGIPVSK MLEAEKEKLL RMEDVLHKRV IGQVEAVEVV SNAIRRSRAG LSDPNRPIGS
     FLFLGPTGVG KTELCKTLAS FMFDSEDAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
     GSTRIQENFG SLDYEGMKEQ VMDVVSKHFR PEFLNRVDES VVFHPLGQDH IKSIASIQLQ
     RLASRMEEKG FVLEVSDKAL EHIAQVGFDP VYGARPLKRA IQQSVENPLA KEILAGNVVP
     DKPIKLVVSN DQIIAHQ
//
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