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
//