ID A0A0A8ENK9_9ACTN Unreviewed; 883 AA.
AC A0A0A8ENK9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=GZL_04835 {ECO:0000313|EMBL:AJC57413.1};
OS Streptomyces sp. 769.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC57413.1, ECO:0000313|Proteomes:UP000031113};
RN [1] {ECO:0000313|EMBL:AJC57413.1, ECO:0000313|Proteomes:UP000031113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=769 {ECO:0000313|EMBL:AJC57413.1,
RC ECO:0000313|Proteomes:UP000031113};
RA Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL Submitted (DEC-2012) 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; CP003987; AJC57413.1; -; Genomic_DNA.
DR RefSeq; WP_039634963.1; NZ_CP003987.1.
DR AlphaFoldDB; A0A0A8ENK9; -.
DR KEGG; stre:GZL_04835; -.
DR HOGENOM; CLU_005070_4_0_11; -.
DR Proteomes; UP000031113; 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};
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 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 516..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 96155 MW; A43DA40E5A08A00A CRC64;
MDAELTNKSR EALSAASERA VAAGHADMTS AHLLLALLAG QDNENIMDLL AAVEADAAQL
RSGAERQLAG LPSVQGSTVA PPQPDRELLA AIADAAQRAK DLGDAYISTE HLLIGIATKG
GRTGELLEQQ GATAKKLLAA FEASRGGQRV TTPDPEGTYK ALEKFGTDFT AAAREGKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLRNKRLVS
LDLGAMVAGA KYRGEFEERL KTVLAEIKAS EGQIITFIDE LHTVVGAGAG GDSAMDAGNM
LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV AEPTVEDTVA ILRGLKGRYE
AHHKVQIADS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVEIDELQRA
VDRLKMEELA LRNETDAGSV ARLEKLRKDL ADKEEELRGL TARWEKEKQS LNRVGELKER
LDDLRGQAER AQRDGDFDTA SKLLYGEIPS LERELAKAAE AEAEQEAAKG SGGAKESMVK
EEVGPDDIAD VVGSWTGIPA GRLLEGETQK LLRMEEELGK RLIGQTEAVA AVSDAVRRTR
AGIADPDRPT GSFLFLGPTG VGKTELAKAL ADFLFDDERA MVRIDMSEYG EKHSVARLVG
APPGYVGYEE GGQLTEAVRR RPYSVVLLDE VEKAHHEVFD VLLQVLDDGR LTDGQGRTVD
FRNTILILTS NLGSNFLMDP LLKEEQKKEK VLETVRSAFR PEFLNRLDDL VVFHPLGTDQ
LERIARIQLD HLQRRLGDRR LTLDVTARAL TWLAWLGRQP VVDAPAPDLS YGARPLRRLV
QTAIGDQLAR AILAGDVLDG DTVRVDVDGD GERLSVAAVR PAA
//