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Database: UniProt
Entry: A0A1V3TR36_9PAST
LinkDB: A0A1V3TR36_9PAST
Original site: A0A1V3TR36_9PAST 
ID   A0A1V3TR36_9PAST        Unreviewed;       858 AA.
AC   A0A1V3TR36;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BMT54_07740 {ECO:0000313|EMBL:OOH88960.1};
OS   Pasteurellaceae bacterium 15-036681.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae.
OX   NCBI_TaxID=1924934 {ECO:0000313|EMBL:OOH88960.1, ECO:0000313|Proteomes:UP000188845};
RN   [1] {ECO:0000313|EMBL:OOH88960.1, ECO:0000313|Proteomes:UP000188845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=15-036681 {ECO:0000313|EMBL:OOH88960.1,
RC   ECO:0000313|Proteomes:UP000188845};
RA   Stuber T.P., Hicks J.A., Robbe-Austerman S., Lantz K.;
RT   "Draft genome sequence of a Pasteurellaceae bacterium isolated from a pygmy
RT   hippo (Hexaprotodon liberiensis).";
RL   Submitted (NOV-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:OOH88960.1}.
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DR   EMBL; MQVI01000025; OOH88960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3TR36; -.
DR   STRING; 1924934.BMT54_07740; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000188845; 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:UP000188845};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          411..498
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   858 AA;  96131 MW;  FDC2BAD1489F7C14 CRC64;
     MNIDKFTNKF QSAIAEAQSL AIGKDNPYIE PAHLMLTLLK QNDGSIAPLV TALNVPVTKL
     ENELDTIINR LPQVQGGNNT QPSQQLIRLL NQCDKLAQQF GDSFISSELF VLAALEDGGD
     LGKLFKQLGL TKEKVTTAIQ NIRGGDSVNS QNAEETRQAL QKYTIDLTDR ARSGKLDPVI
     GRDEEIRRAV QVLQRRTKNN PVLIGEPGVG KTAIVEGLAQ RIVNNEVPEG LKNKRVLSLD
     MGALIAGAKY RGEFEERLKA VLNELAKEEG QVILFIDEIH TMVGAGKTDG AMDAGNLLKP
     SLARGELHCV GATTLDEYRQ YIEKDAALER RFQKVLVDEP TVEDTIAILR GLKERYEIHH
     HVQITDPAIV AAATLSHRYI SDRQLPDKAI DLIDEAASSV RMEIDSKPEP LDRLERRIIQ
     LKLEQQALQK EDDEASRQRL TKLIEDLTAR EREYAELEEV WKAEKSALLG TQHIKEELEN
     ARLKMEQARR ENNFEKMAEL QYGIIPSLEK QLKEAEKHEG EESENKLLRT RVTDEEIAEV
     LSKATGIPVS KMMEGEKEKL LKMEEVLHKR VIGQGEAVDA VANAIRRSRA GLSDPNRPIG
     SFLFLGPTGV GKTELCKTLA TFLFDSEDAM VRIDMSEFME KHSVSRLVGA PPGYVGYEEG
     GYLTEAVRRR PYSVILLDEV EKAHPDVFNI LLQVLDDGRL TDGQGRTVDF RNTVVIMTSN
     LGSHLIQENA ENMNYDEMKE IVMSVVGQHF RPEFINRIDE TVVFHPLDKE NIRAIARIQL
     QRLIKRMAER GYNVTVTDAA VDHIGAAGFD PLFGARPLKR AIQQEVENSL AQQILSGKLL
     PNRDVTIDYQ DDRIVAVQ
//
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