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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//