ID A0A0G1F507_9BACT Unreviewed; 624 AA.
AC A0A0G1F507;
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=UV58_C0014G0014 {ECO:0000313|EMBL:KKS81968.1};
OS Candidatus Wolfebacteria bacterium GW2011_GWC1_43_10.
OC Bacteria; Candidatus Wolfebacteria.
OX NCBI_TaxID=1619011 {ECO:0000313|EMBL:KKS81968.1, ECO:0000313|Proteomes:UP000034810};
RN [1] {ECO:0000313|EMBL:KKS81968.1, ECO:0000313|Proteomes:UP000034810}
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:KKS81968.1}.
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DR EMBL; LCFA01000014; KKS81968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1F507; -.
DR PATRIC; fig|1619011.3.peg.561; -.
DR Proteomes; UP000034810; 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 597..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 525..585
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 597..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 624 AA; 68005 MW; FDF57345F4F88292 CRC64;
MAKILGIDLG TTNSAMAIVE GGEPKVLENA EGNRTTPSVV AVSKSGGRLV GLLAKRQAVV
NPKNTIFSVK RLIGRKFSDK EVQHDAKWLP FDMQASSSGG VEVKIGDPSA GSGQVKWYKP
EEISAMILAK LKADAENYLG EKIEEAVITV PAYFDDSQRQ STKNAGEIAG LKVRRIINEP
TAAALAYGLN RQKNEKIVVY DFGGGTFDVS VLEIGDDVVE VKSTGGDTHL GGDDIDKIIM
DYLVNEYKKN EGIDLSKDPL ALQRLKEAAE KAKHELSTVV EAEINLPYIT SDANGPKHFL
MKLTRAKLEE LVVKLVDKSV DIVKQVVKDS GLSLSDVNEI ILVGGQTRMP LIQEKVKSLF
GKEPHKGINP DEVVAVGAAV QAGIFQGDVK DVLLLDVIPL SLGIETLGGV FTPIIEKNTT
VPTSRSQIFS TAADNQTSVE IHVLQGERPM ATDNKTLARF ILDGIPPSPR GLPQIEVTFD
IDANGILHVS AKDKATSKVQ SVKIEASTQL SKDEVEKLKQ EAVAHAEEDR QKKELVETKN
QAEQIIYLAQ KNLEEWKDKI PPQTKESISQ KIEDLKKSLE SNDRETIQSK LSELSSELQN
IGKGMYNQKE EPSSGDTGEE QSKE
//
