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Database: UniProt
Entry: A0A1S1NWB2_9GAMM
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ID   A0A1S1NWB2_9GAMM        Unreviewed;       873 AA.
AC   A0A1S1NWB2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BH688_06895 {ECO:0000313|EMBL:OHV11484.1};
OS   Kushneria phosphatilytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Kushneria.
OX   NCBI_TaxID=657387 {ECO:0000313|EMBL:OHV11484.1, ECO:0000313|Proteomes:UP000179907};
RN   [1] {ECO:0000313|EMBL:OHV11484.1, ECO:0000313|Proteomes:UP000179907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCWA18 {ECO:0000313|EMBL:OHV11484.1,
RC   ECO:0000313|Proteomes:UP000179907};
RA   Wang C., Qu L.;
RT   "The draft genome suquence of Kushneria sp. YCWA18.";
RL   Submitted (OCT-2016) 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:OHV11484.1}.
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DR   EMBL; MKZT01000007; OHV11484.1; -; Genomic_DNA.
DR   RefSeq; WP_070977940.1; NZ_MKZT01000007.1.
DR   AlphaFoldDB; A0A1S1NWB2; -.
DR   STRING; 657387.BH688_06895; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000179907; 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:UP000179907};
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          434..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   873 AA;  97010 MW;  7DC45C127616CD5D CRC64;
     MRIDRLTSKL QNALSEAQSL AVGRSHNELQ PGHLLLALFD SRDSGMRALI QKAGGDPARV
     REGLISHLDN LPTVKNFDGN VAMSQDLGRL FNFADREAQN RGDQYVATEL VLLAALEMNH
     AVTRVLTGAG LSRTSVRQAI DELRGGDTVN DAEAEEQREA LDKYTTDLTA RAEEGKLDPV
     IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKDKRVLAL
     DLGALLAGAK YRGDFEERLK GVLNELAKEE GRVILFIDEL HTMVGAGKTE GSMDAGNMLK
     PALARGELHC VGATTLDEYR HDIEKDAALE RRFQKVLVDE PTEEDTVAIL RGLKERYEVH
     HGVDITDGAI IAAAKLSQRY ITDRQLPDKA IDLIDEAASR IRMELDSKPE EMDRLDRRLI
     QLKMEREAPR KETDDATRKR LEHLEAQIDE LEREYADLDE VWKAEKASIQ GAAQFKAELE
     QARTDLEAAR RQGDLGRMSE LQYGVIPSLE KKIADSSDAE ADTASHQLLR SNVTEEEVAE
     VVSRWTGIPV AKMLEGEREK LLRMEEALHE RVIGQDEAVS AVANAVRRSR AGISDPNRPN
     GSFLFLGPTG VGKTELCKTL ANFLFDTEEA MVRLDMSEFM EKHSVSRLIG APPGYVGYDQ
     GGYLTEAVRR KPYSVLLLDE VEKAHPDVFN ILLQVLEDGR LTDGQGRTVD FRNTVVVMTS
     NLGSGVIQSY AGETDEDGYE RMKAAVMDEV ANHFRPELIN RIDEVVVFHA LGQEQIQQIA
     DIQLSRLRNR LAERDMALEV SSDAMAQLAV VGFDPVYGAR PLKRAIQNRI ENPLAQELLA
     GHYSAGDTIR VSAEEDHLKF ERVNRSEDVT AAK
//
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