GenomeNet

Database: UniProt
Entry: A0A1P8UHY0_9GAMM
LinkDB: A0A1P8UHY0_9GAMM
Original site: A0A1P8UHY0_9GAMM 
ID   A0A1P8UHY0_9GAMM        Unreviewed;       863 AA.
AC   A0A1P8UHY0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BW247_10125 {ECO:0000313|EMBL:APZ43404.1};
OS   Acidihalobacter ferrooxydans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ43404.1, ECO:0000313|Proteomes:UP000243807};
RN   [1] {ECO:0000313|EMBL:APZ43404.1, ECO:0000313|Proteomes:UP000243807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V8 {ECO:0000313|EMBL:APZ43404.1,
RC   ECO:0000313|Proteomes:UP000243807};
RA   Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA   Watkin E.L.J.;
RT   "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT   V8).";
RL   Submitted (JAN-2017) 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   ---------------------------------------------------------------------------
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; CP019434; APZ43404.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8UHY0; -.
DR   STRING; 1765967.BW247_10125; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000243807; Chromosome.
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:UP000243807};
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          405..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   863 AA;  95713 MW;  8CB3CE6036DCC43C CRC64;
     MRMDKLTSKF QMALADAQSL AVGRDHQFIE PLHLMRALLD QEGGTVRPLL TKAGVNVNQL
     RARLDEALDS LPSVEGTGGD VHVSNELGNL LNLTDKLAQK RQDAYISSEL FLLAVLDGKG
     HLHDLLTQAG GVRGAIEKAI DEMRGGATVD DPNAEDSRKA LEKYTIDLTE RAEQGKLDPV
     IGRDEEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVDGAVPE GLKSKRVLSL
     DLGALLAGAK FRGDFEERLK AVLNDLSKQE GRIILFIDEI HTMVGAGKAE GAMDAGNMLK
     PALARGELHC IGATTLDEYR KYIEMDAALE RRFQKVLVDE PSVEDTIAIL RGLKERYEVH
     HGVEITDPAI VAAAMLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE EMDRLERRLI
     QLKIEREALK KESDEASKKR LADLEEQIAK LEREFSDLDE IWKSEKAAVQ GATHIKEELE
     RVRTELETAR RAGDLGRMSE LQYGRIPELE RQLAMASQAE MQEMTLLRNK VSDEEIAEVV
     SRWTGIPVSK MLEGEKEKLL RMEDVLGQRV VGQNEAVKAV ANAIRRSRAG LSDPNRPNGS
     FLFLGPTGVG KTELTKSLAS FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
     GSQTIQELAG EENYEAMKAA VMEVVGGHFR PEFINRIDEV VVFHPLGREQ IRAITRIQLD
     YLRRRLADRD MGLEISDAAL DRLGEAGFDP VYGARPLKRA IQQDVENPLA QAILGGEFLP
     GDVIYVDAGE TGLNFSTIAT DAA
//
DBGET integrated database retrieval system