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Database: UniProt
Entry: W7PZB3_9GAMM
LinkDB: W7PZB3_9GAMM
Original site: W7PZB3_9GAMM 
ID   W7PZB3_9GAMM            Unreviewed;       860 AA.
AC   W7PZB3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=Q427_16860 {ECO:0000313|EMBL:EWH00912.1};
OS   Halomonas sp. BC04.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1403540 {ECO:0000313|EMBL:EWH00912.1, ECO:0000313|Proteomes:UP000019279};
RN   [1] {ECO:0000313|EMBL:EWH00912.1, ECO:0000313|Proteomes:UP000019279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC04 {ECO:0000313|EMBL:EWH00912.1,
RC   ECO:0000313|Proteomes:UP000019279};
RA   Farooqui S., Greene A.C., Patel B.K.;
RT   "Draft Genome Sequence of Halomonas Strain BC04, an Aromatic-degrading
RT   moderate Halophilic Bacterium.";
RL   Submitted (DEC-2013) 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:EWH00912.1}.
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DR   EMBL; AZQX01000194; EWH00912.1; -; Genomic_DNA.
DR   RefSeq; WP_043514801.1; NZ_AZQX01000194.1.
DR   AlphaFoldDB; W7PZB3; -.
DR   PATRIC; fig|1403540.3.peg.3154; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000019279; 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:UP000019279};
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   860 AA;  96057 MW;  8883FD39D8F570A9 CRC64;
     MRFDKFTGKL QNAVADAQSL AVGRGHNQLD PGHLLLALLD ASDTGVKALI QRADGDPARL
     RDSLVGYLDD LPQVSQFEGE VQPSRNLIKL FNLTDREAQK RGDQYIASEL VLLAALEMRH
     GVSKLLTQAG VTRKSLETAI DSLRGGERVD DPNAEEQREA LEKYTLDLTE RAASGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVDGEVPE GLKNKRVLSL
     DMGSLLAGAK FRGEFEERLK SVLKELSQEE GQVILFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC VGATTLNEYR QHIEKDAALE RRFQKVLVEE PSEEDTVAIL RGLKERYEVH
     HGVDITDGAI IAAAKLSTRY ITDRQLPDKA IDLIDEASSR IRMELDSKPE EMDRLDRRLI
     QLKMEREHLK KETDEASRKR LESLQAQIDE LEREYADLDE IWKAEKASIQ GAAQYKDELD
     KVRTDLEQAR RQGDLARMSE LQYGVIPELE RKIAESSEAE ADTSRHQLLR SNVTEEEIAE
     VVSRWTGIPV AKMLEGERDK LLRMEESLHE RVIGQDEAVT AVANAVRRSR AGLSDPNRPN
     GSFLFLGPTG VGKTELCKAL ANFLFDTEES MVRIDMSEFM EKHSVARLIG APPGYVGYEE
     GGYLTEAVRR RPYSVLLLDE VEKAHADVFN ILLQVLEDGR LTDGQGRTVD FRNTVIVMTS
     NMGSDIIQRM GGDDSDYEQM KEMVMAVVGD HFRPELINRI DEVVVFHALM QEQIQAIAGI
     QLDRLRARLA EHQLELDVSD EALAQLAVVG FDPVYGARPL KRAIQSRIEN PLAQDLLAGK
     FRPGDVIRVT VENGKLSFNT
//
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