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Database: UniProt
Entry: A0A429UVM2_9ACTN
LinkDB: A0A429UVM2_9ACTN
Original site: A0A429UVM2_9ACTN 
ID   A0A429UVM2_9ACTN        Unreviewed;       871 AA.
AC   A0A429UVM2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RST23852.1};
GN   ORFNames=EF908_08595 {ECO:0000313|EMBL:RST23852.1};
OS   Streptomyces sp. WAC04770.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2487423 {ECO:0000313|EMBL:RST23852.1, ECO:0000313|Proteomes:UP000282152};
RN   [1] {ECO:0000313|EMBL:RST23852.1, ECO:0000313|Proteomes:UP000282152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC04770 {ECO:0000313|EMBL:RST23852.1,
RC   ECO:0000313|Proteomes:UP000282152};
RA   Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT   "Unmasking the antibiotic production potential of Actinomycetes through
RT   CRISPR/Cas9 inactivation of ubiquitous gene clusters.";
RL   Submitted (NOV-2018) 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:RST23852.1}.
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DR   EMBL; RQIR01000394; RST23852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429UVM2; -.
DR   Proteomes; UP000282152; 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:UP000282152};
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          846..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          414..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  94972 MW;  3A4E305C47DB22BA CRC64;
     MDAELTNKSR DAINAAGDRA VKDGHPDLTP GHLLLALLGG QDNENITDLL AAVEADQAVV
     RAGTEKLLGS LPSVTGSTVA PPQPNRELLA VIQDAAQRAK ELGDEYLSTE HLLIGIAAKG
     GRAGEILDGQ GATAKKLLAA FETSRGGRRV TTPDPEGQYK ALEKFGTDFT AAARDGKLDP
     VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKNKRLVS
     LDLGAMVAGA KYRGEFEERL KTVLSEIKES DGQIITFIDE LHTVVGAGAG GDSAMDAGNM
     LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV AEPSVEDTIA ILRGLKGRYE
     AHHKVQIADS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PLEIDELQRS
     VDRLRMEELA LKNESDAASK QRLEKLRRDL ADKEEELRGL NARWEKEKQG LNRVGELKER
     LDELRGQAER AQRDGDFDAA SKLLYGEIPG LERELEEAAE AEQEASKDTM VKEEVGPDDI
     ADVVGAWTGI PAGRLLEGET QKLLRMESEL GKRLIGQTEA VQAVSDAVRR TRAGIADPDR
     PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMIRIDMSE YGEKHSVARL VGAPPGYVGY
     EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDILLQVLDD GRLTDGQGRT VDFRNTILVL
     TSNLGSQFLM DPLVKPEVKK EQVLEVVRAS FKPEFINRLD DLVVFSALSG DELAHIAGLQ
     IDRLAKRLAD RRLTLDVTPE ALAWLAQEGN DPAYGARPLR RLIQTAIGDR LAKEILSGEI
     RDGDTVRVDR AREEDEGGLT VGPVSPASPA S
//
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