ID A0A0G0XFD1_9BACT Unreviewed; 633 AA.
AC A0A0G0XFD1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332};
GN ORFNames=UU32_C0015G0003 {ECO:0000313|EMBL:KKR86452.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_41_10.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618577 {ECO:0000313|EMBL:KKR86452.1, ECO:0000313|Proteomes:UP000033858};
RN [1] {ECO:0000313|EMBL:KKR86452.1, ECO:0000313|Proteomes:UP000033858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC ECO:0000256|RuleBase:RU003322}.
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:KKR86452.1}.
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DR EMBL; LCAE01000015; KKR86452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0XFD1; -.
DR PATRIC; fig|1618577.3.peg.249; -.
DR Proteomes; UP000033858; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00332}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00332};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 593..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 498..527
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 611..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 196
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 633 AA; 68546 MW; E3CC9EAC79F199B8 CRC64;
MGKIVGIDLG TTNSVVAVME GGRPKVIPAA DTGRNITPSV VEPVKNLVGD VAKRQVVLNP
KNTIYSIKRL MGRRHDDKEV ERTKKMVPYE IVSGKDGGAD VEVEGKNYTP QEISARILMK
LKKDAETYLG ERVEQAVITV PAYFDDSQRH ATKQAGEIAG FKVERIINEP TAAALAYGLD
KKHAEKIAVY DLGGGTFDIS ILELGEGVFE VKATNGDTHL GGDDFDEVIV DYIASEFKKE
NTVDLRGDKQ ALQRVRDAAE KAKIELSAAD EVEINQPYIT QKDGQPMHLT MKLTRAKLEN
LVSDLIEKTM KPVSDCLKDA KLDPHDIDEV ILVGGMTRMP KVVETVKNFF EKDPNKSVNP
DEVVAIGAAI QAGVLGGEVK DILLLDVTPL TLAIETLGGV ATPMIPRNTT VPTSKTETFS
TAADNQTQVQ IVVTQGERPM SADNKTLGTF TLDGIPPAPR GVPQIEVTFD MDASGILTVT
AKDKATGKTT NIKITGAVGL SDDEIKRMQA EAEKHKEEDE KKAETIKTKN NADSMVATAE
KALKDAGDKV DAKIKEQVEE KIKKVKEVVG KDISTKEEIE SATKDLSDTL SQVGQVMYGS
TGSPSGDAAD PEPVEGEKKD EKKEKVEEGE VVE
//
