ID A0A6B3AE43_9ACTN Unreviewed; 865 AA.
AC A0A6B3AE43;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:NEC27149.1};
GN ORFNames=G3I20_11400 {ECO:0000313|EMBL:NEC27149.1};
OS Streptomyces sp. SID8111.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2706100 {ECO:0000313|EMBL:NEC27149.1, ECO:0000313|Proteomes:UP000472955};
RN [1] {ECO:0000313|EMBL:NEC27149.1, ECO:0000313|Proteomes:UP000472955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SID8111 {ECO:0000313|EMBL:NEC27149.1,
RC ECO:0000313|Proteomes:UP000472955};
RA Currrie C., Chevrette M., Carlson C., Stubbendieck R., Wendt-Pienkowski E.;
RT "Insect and environment-associated Actinomycetes.";
RL Submitted (JAN-2020) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NEC27149.1}.
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DR EMBL; JAAGMY010000338; NEC27149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6B3AE43; -.
DR Proteomes; UP000472955; 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: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:UP000472955};
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 440..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 94680 MW; DDDB0BA00D838663 CRC64;
MDAELTNRSR DAINAAGNRA VTEGHPDLTP AHLLLALLQG QDNENITDLL AAVDADQAAV
RSGAERVLAG LPSVTGSTVA PPQPNRELLA VIADAQARAR DLGDEYLSTE HLLIGIAAKG
GAAGEVLSQQ GATANKLQEA FQRTRGSRRV TTADPEGQYK ALEKFGTDLT AAAREGRLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKDKRLVA
LDLGAMVAGA KYRGEFEERL KTVLAEIKES DGQVVTFIDE LHTVVGAGAG GDSAMDAGNM
LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV AEPSVEDSIA ILRGLKGRYE
AHHKVQIADS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVEIDELQRS
VDRLKMEELA IGKETDPASR ERLEKLRRDL ADKEEELRGL TARWEKEKQS LNRVGELKEK
LDELRGQAER AQRDGDFDTA SKLLYGEIPS LERDLEAASE AEEEVARDTM VKEEVGSDDI
ADVVASWTGI PAGRLLEGET QKLLRMEDEL GKRLIGQTEA VRAVSDAVRR SRAGVADPDR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRVDMSE YSEKHSVARL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDILLQVLDD GRLTDGQGRT VDFRNTILVL
TSNLGSQFLV DPLTSETEKK EQVLEVVRAS FKPEFLNRLD DLVVFSALTK PELERIAALQ
IDRLARRLAE RRLTLDVTDE ALAWLADEGN DPAYGARPLR RLVQTAIGDR LAKEILSGEI
RDGDTVRVDR FGDELIVGPA TGKTL
//