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}.
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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
//