ID A0A101UC86_9ACTN Unreviewed; 865 AA.
AC A0A101UC86;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=AQJ58_32610 {ECO:0000313|EMBL:KUO08098.1};
OS Streptomyces sp. DSM 15324.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO08098.1, ECO:0000313|Proteomes:UP000053431};
RN [1] {ECO:0000313|EMBL:KUO08098.1, ECO:0000313|Proteomes:UP000053431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO08098.1,
RC ECO:0000313|Proteomes:UP000053431};
RA Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
RL Submitted (OCT-2015) 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|ARBA:ARBA00004496,
CC 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:KUO08098.1}.
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DR EMBL; LMXA01000034; KUO08098.1; -; Genomic_DNA.
DR RefSeq; WP_067256677.1; NZ_KQ949034.1.
DR AlphaFoldDB; A0A101UC86; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000053431; 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 78, MITOCHONDRIAL; 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:UP000053431};
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 436..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 94275 MW; 06E77395A6AC3AE5 CRC64;
MDAELTNRSR DAINAASNRA VSGGHPDLTP AHLLLALLQG QDNENIVDLL AAVGADQAAV
RAGTEHVLAG LPSVTGSTVA PPQPNRELLA VIADAQARAQ ELGDEFLSTE HLLIGTAAKG
GQAADVLGRH GAGPDRLQDA FRKARGGRRV TTADPEGQYK ALEKFGTDFT AAARDGKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKDKRLVS
LDLGAMVAGA KYRGEFEERL KTVLAEIKDS DGQIITFIDE LHTVVGAGAG GDSAMDAGNM
LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV AEPTVEDTIA ILRGLKGRYE
AHHKVQIADS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVEIDELQRS
VDRLKMEELA IGKETDAASR ERLEKLRRDL ADKEEELRGL TARWEKEKQS LNRVGELKEK
LDDLRGQAER AQREADFDTA GKLLYGEIPA LERDLEAATE AEEEAARGTM VKEEVGSDDI
ADVVAAWTGI PAGRLLEGET QKLLRMEAEL GRRLIGQAEA VQAVSDAVRR SRAGIADPDR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMIRIDMSE YGEKHSVARL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDVLLQVLDD GRLTDGQGRT VDFRNAILVL
TSNLGSQYLV DPVSTEAEKK EQVLEVVRAS FKPEFLNRLD DLVVFSALSK DELGRIARLQ
IDRLARRLAD RRLTLEVTDA ALAWLADEGN DPAYGARPLR RLVQTAIGDR LAREILSGEV
KDGDTVRVDT FGEDLIVGPK PTKTL
//
