GenomeNet

Database: UniProt
Entry: A0A1P8XTI3_9ACTN
LinkDB: A0A1P8XTI3_9ACTN
Original site: A0A1P8XTI3_9ACTN 
ID   A0A1P8XTI3_9ACTN        Unreviewed;       880 AA.
AC   A0A1P8XTI3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BV401_14560 {ECO:0000313|EMBL:AQA11526.1};
OS   Streptomyces autolyticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA11526.1, ECO:0000313|Proteomes:UP000187851};
RN   [1] {ECO:0000313|Proteomes:UP000187851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA   Yin M., Jiang M., Lu T.;
RT   "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
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; CP019458; AQA11526.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8XTI3; -.
DR   STRING; 75293.BV401_14560; -.
DR   KEGG; sauo:BV401_14560; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000187851; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          87..121
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          417..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   880 AA;  98215 MW;  2A80B146A7E838C0 CRC64;
     MDMNRLTQKS QEALQDAQTR AQRYGHTEVD GEHLLLALLD QPEGLTPRLI GQLGADPDAV
     RTMLEAELAR KPKVTGPGAT PGQIFATQRL GQVLDTAERE AKRLKDEYVS VEHLVLALTE
     EGSATAAGRV LKEHGVTKEA FLHALTQVRG SQRVTSANPE VAYEALEKYG RDLVLEARSG
     KLDPVIGRDA EIRRVTQILS RKSKNNPVLI GDPGVGKTAI VEGLAQRIVR GDVPEGLRDK
     TIFALDMGSL VAGAKYRGEF EERLKAVLTE VTSAQGRILL FVDELHTVVG AGAAEGAMDA
     GNMLKPMLAR GELHMIGATT LDEYRKHIEK DAALERRFQM VLVDEPSVED TVSILRGLRE
     RLEVFHGVKI QDTALVSAAT LSHRYISDRF LPDKAIDLVD EACARLRTEI DSMPAELDEI
     TRRVTRLEIE EAALSKESDA ASRQRLEELR RELADLRAEA DAKHAQWEAE RQSIRRVQDL
     RRELEEVRLE AEEAERAYDL NRAAELRYGR LQELERKLAA EEEQLATRQG THRLLREVVT
     EEEIADIVSA WTGIPVSRLK EGEREKLLRL DQILQERVIG QDEAVKLVSD AIIRARSGIR
     DPRRPIGSFI FLGPTGVGKT ELAKALAAAL FDTEENMIRL DMSEYQERHT VSRLVGAPPG
     YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HTDVFNTLLQ VLDDGRITDA QGRLVDFRNT
     VIIMTSNIGS MHLLDGVTAQ GELKPDARSL VMSELRGHFR PEFLNRVDDI VLFKPLGEPQ
     IERIVELQLD ELRKRLAERL ITIELTPAGR EVIAHEGYDP VYGARPLRRY ISHEVETLIG
     RALLRGDIEE GATVKVDGRH GELTVTYERR PETAGLGKAA
//
DBGET integrated database retrieval system