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Database: UniProt
Entry: L8JDC5_9GAMM
LinkDB: L8JDC5_9GAMM
Original site: L8JDC5_9GAMM 
ID   L8JDC5_9GAMM            Unreviewed;       857 AA.
AC   L8JDC5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=C942_01205 {ECO:0000313|EMBL:ELR65417.1};
OS   Photobacterium marinum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR65417.1, ECO:0000313|Proteomes:UP000011134};
RN   [1] {ECO:0000313|EMBL:ELR65417.1, ECO:0000313|Proteomes:UP000011134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK15 {ECO:0000313|EMBL:ELR65417.1,
RC   ECO:0000313|Proteomes:UP000011134};
RA   Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT   "Genome Assembly of Photobacterium sp. AK15.";
RL   Submitted (DEC-2012) 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:ELR65417.1}.
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DR   EMBL; AMZO01000019; ELR65417.1; -; Genomic_DNA.
DR   RefSeq; WP_007466432.1; NZ_AMZO01000019.1.
DR   AlphaFoldDB; L8JDC5; -.
DR   PATRIC; fig|1056511.3.peg.2699; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000011134; 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   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..468
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   857 AA;  96111 MW;  C41F788618E9C08E CRC64;
     MRLDRFTSKF QMAISDAQSL ALGRDHQYIE PAHLMVALLN QDGSTIRPLL TMLNIDVSQL
     RSGLSEILDR QPKVTGIGGD VQLSHGMGML LNICDKLAQK RKDKYISSEL FILAAIDDKG
     PLGQLLKDKG LTAEKVEKAI EQVRGGQNVD DPNAEENRQA LKKFTIDLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVIIGEPGV GKTAIVEGLA QRIVNGEVPE GLRHKRVLSL
     DMGALIAGAK YRGEFEERLK AVLNELSQEE GNIILFIDEL HTMVGAGKGE GSMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVEE PTVEDTVAIL RGLKERYELH
     HHVEITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRMQIDSKPE SLDRLERRII
     QLKIEQQALV KESDDASHKR LKDLSEELDK KEREYAELEE VWNAEKAALS GTQHIKTELE
     QARTDMEIAR RAGDLNRMSE LQYGKIPELE KQLDLAAQAE MQEMSLLKNK VTDAEIAEVL
     SRQTGIPVAK MLEGEREKLL HMEEALHKRV IGQDEAVDAV ANAIRRSRAG LSDPNRPIGS
     FLFLGPTGVG KTELCKSLAN FMFDSEDAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NSVIIMTSNL
     GSDRIQEHFG ELDYDGIKHT VMEVVGQHFR PEFINRVDET VVFHPLGQEH IKNIANIQIM
     RLVKRLEEKD YQLELQESAL ELISQAGFDP VYGARPLKRA IQHYIENPLA QDILSGKFTT
     GKPIKLLAEN EQIVAQQ
//
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