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Database: UniProt
Entry: A0A1E5DYX1_9VIBR
LinkDB: A0A1E5DYX1_9VIBR
Original site: A0A1E5DYX1_9VIBR 
ID   A0A1E5DYX1_9VIBR        Unreviewed;       858 AA.
AC   A0A1E5DYX1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=A1QC_13555 {ECO:0000313|EMBL:OEF22559.1};
OS   Vibrio rumoiensis 1S-45.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1188252 {ECO:0000313|EMBL:OEF22559.1, ECO:0000313|Proteomes:UP000094070};
RN   [1] {ECO:0000313|EMBL:OEF22559.1, ECO:0000313|Proteomes:UP000094070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1S-45 {ECO:0000313|EMBL:OEF22559.1,
RC   ECO:0000313|Proteomes:UP000094070};
RX   PubMed=22955834; DOI=10.1126/science.1219385;
RA   Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA   Le Roux F., Mincer T., Polz M.F.;
RT   "Ecological populations of bacteria act as socially cohesive units of
RT   antibiotic production and resistance.";
RL   Science 337:1228-1231(2012).
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:OEF22559.1}.
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DR   EMBL; AJYK02000115; OEF22559.1; -; Genomic_DNA.
DR   RefSeq; WP_017023711.1; NZ_AJYK02000115.1.
DR   AlphaFoldDB; A0A1E5DYX1; -.
DR   STRING; 1188252.A1QC_13555; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000094070; 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:UP000094070};
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;  95555 MW;  90176F50DA27CB0C CRC64;
     MRFDKFTSKF QLAISDAQSL ALGRDHQFIE PVHLMQALLN QDGSTIRPIF TMLGVDGTQL
     RSKLSQELDK LPKVTGTGGD VQLSKTLGNL LNLCDQFAQQ RKDAYISSEI FLLAAVEDRG
     ALGKLFKDLG LTKDKVAKAI DEIRGGQNVD DPNAEEKRQA LEKYTIDLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGQPGV GKTAIVEGLA LRIINNEVPE GLRGRRVLSL
     DMGALIAGAK YRGEFEERLK AVLNELAQED GNIILFIDEL HTMVGAGKGE GSMDAGNMLK
     PALARGELHC VGATTLDEYR QYVEKDPALE RRFQKVLVDE PSVEDTIAIL RGLKERYELH
     HHVEITDPAI VAAATLSHRY VSDRQLPDKA IDLIDEAASS IRIQMDSKPE SLDKLDRRII
     QLKIEQQALL NESDAASTKR LEILNQELTE KEREYSELEE VWKTEKAALS GTQHIKTELE
     QARLDMDVAR RAGDLQRMSE LQYGKIPELE KQLEIASQAE TIEMTLLKNR VTDAEIAEVL
     SKQTGIPVSK MLEAEKAKLL SMETVLHERV IGQKEAVEVV SNAIRRSRAG LSDPNKPIGS
     FLFLGPTGVG KTELCKTLAS FMFDSADAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFK NTVVIMTSNL
     GSDRIQEKAA TSTYDSMKAE VMEIVSQHFR PEFLNRVDES VVFHPLGQEQ IKSIASIQLE
     RLSQRMAEKE YILDVGDDAL ELVAQVGFDP VYGARPLKRA IQQMVENPLA RSILSGELIP
     GQTVHLTVKD DQIVANQS
//
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