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
//