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Database: UniProt
Entry: A0A0J1H453_9GAMM
LinkDB: A0A0J1H453_9GAMM
Original site: A0A0J1H453_9GAMM 
ID   A0A0J1H453_9GAMM        Unreviewed;       857 AA.
AC   A0A0J1H453;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-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=ABT57_19370 {ECO:0000313|EMBL:KLV06556.1};
OS   Photobacterium ganghwense.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV06556.1, ECO:0000313|Proteomes:UP000035909};
RN   [1] {ECO:0000313|EMBL:KLV06556.1, ECO:0000313|Proteomes:UP000035909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV06556.1,
RC   ECO:0000313|Proteomes:UP000035909};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-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:KLV06556.1}.
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DR   EMBL; LDOU01000021; KLV06556.1; -; Genomic_DNA.
DR   RefSeq; WP_047886902.1; NZ_PYMI01000015.1.
DR   AlphaFoldDB; A0A0J1H453; -.
DR   STRING; 320778.ABT57_19370; -.
DR   PATRIC; fig|320778.3.peg.4186; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000035909; 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:UP000035909};
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;  95734 MW;  BE425DE1FCF76C72 CRC64;
     MRLDRFTSKF QMAISDAQSL ALGRDHQYIE PVHLMTALLN QDGSTIRPLL TLLNVDVAQL
     RSGLAEQLDR LPKVSGIGGD VQLSHGLGVL LNMCDKLAQK RKDKFISSEL FILAAVDDKG
     PLGKLLKDMG MTADKIEKAI EKVRGGQNVD DQNAEENRQA LEKYTINLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLRNKRVLSL
     DMGALIAGAK YRGEFEERLK AVLNELAQEE GSVILFIDEL HTMVGAGKGE GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PSVEDTVAIL RGLKERYELH
     HHVEITDPAI VAAASLSHRY VSDRQLPDKA IDLIDEAASS IRMQIDSKPE SLDRLERRII
     QLKIEQQAIA KESDEASKKR LSDLLEELDS KEREYAELEE VWNAEKAALS GTQHIKAELE
     QARTDMEIAR RAGDLNRMSE LQYGKIPELE KQLDLAAQAE MQEMTLLKNK VTDAEIAEVL
     SRQTGIPVAK MLEGERDKLL RMEEALHKRV IGQNEAVDAV SNAIRRSRAG LSDPHRPIGS
     FLFLGPTGVG KTELCKALAH FMFDSDDAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
     GSDRIQEHFG ELDYEGMKQT VMEVVTHHFR PEFINRVDET VVFHPLGEEH IKNIASIQVT
     RLVKRLEERD YQLDMKDSAL ELIAEAGFDP VYGARPLKRA IQQYVENPLA QDILSGKFVP
     GKPIILEAVD GKISAHQ
//
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