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Database: UniProt
Entry: A0A1I6TBY1_9PSEU
LinkDB: A0A1I6TBY1_9PSEU
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ID   A0A1I6TBY1_9PSEU        Unreviewed;       861 AA.
AC   A0A1I6TBY1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05660874_03860 {ECO:0000313|EMBL:SFS86706.1};
OS   Saccharopolyspora flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=95161 {ECO:0000313|EMBL:SFS86706.1, ECO:0000313|Proteomes:UP000198852};
RN   [1] {ECO:0000313|EMBL:SFS86706.1, ECO:0000313|Proteomes:UP000198852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44771 {ECO:0000313|EMBL:SFS86706.1,
RC   ECO:0000313|Proteomes:UP000198852};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOZX01000006; SFS86706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6TBY1; -.
DR   STRING; 95161.SAMN05660874_03860; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198852; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:SFS86706.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFS86706.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          414..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   861 AA;  93524 MW;  1A1689231ACCD337 CRC64;
     MDAFNPTTKT QQAISSAVQA ATVAGNPDVG PAHLLGALLA QGDGLTAPLL TAVGAEVADV
     RRELESLMNS LPAATGSTVG APQLSGEAVK ALTSAQRLAT EMGDEYVSTE HLLVGLAAEG
     GRVADLLRRH GGTPDALREA FAKVRGSARV TSPDPEGTYQ ALEKYGQDLT ERARAGELDP
     VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVAGDVP ESLRGKRVVA
     LDLGSMVAGA KYRGEFEERL KAVLKEITDS AGQVITFIDE LHTIVGAGAS GEGAMDAGNM
     IKPMLARGEL RMVGATTLDE YREHIETDAA LERRFQQVLV GEPSPEDAVA ILRGLKERYE
     VHHGVRITDG ALVAAATLSD RYITARFLPD KAIDLVDEAA SRLRMEIDSR PVEIDEVERA
     VRRLEIEEMA LAKESDPASV ERLAALRAEL ADKREKLSEL TARWQQEKES IDKVRDLKTQ
     LEQVRGESER AERDGDLGKA AELRYGRIPA LEKELETATR AQSERKAMLQ EEVTADDVAS
     VVSAWTGIPA GRLMEGETAK LLRMEEALGA QVVGQDEAVR AVSDAVRRTR AGVADPDRPT
     GSFLFLGPTG VGKTELAKAL AGFLFDDERS MIRIDMSEYS EKHSVSRLVG APPGYVGHDQ
     GGQLTESVRR RPYSVVLFDE VEKAHSDVFD VLLQVLDDGR LTDGQGRTVD FRNTILVLTS
     NLGSQAIADP NLDERDRDEA VMSVVRGHFK PEFLNRLDDV VVFHQLNTEE LTSIVDIQVD
     RLAARLAQRR LTLDVQPAAR DWLALNGFDP VYGARPLRRL VQTAIGDQLA RKLLAGDIRE
     GDKVRIDVTD DTESLTVTPQ N
//
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