ID A0A0T5ZD03_9ARCH Unreviewed; 620 AA.
AC A0A0T5ZD03;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=XU09_C0010G0020 {ECO:0000313|EMBL:KRT60406.1};
OS Thaumarchaeota archaeon CSP1-1.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1640512 {ECO:0000313|EMBL:KRT60406.1, ECO:0000313|Proteomes:UP000051388};
RN [1] {ECO:0000313|EMBL:KRT60406.1, ECO:0000313|Proteomes:UP000051388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-1 {ECO:0000313|EMBL:KRT60406.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|HAMAP-Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|HAMAP-Rule:MF_00332, 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:KRT60406.1}.
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DR EMBL; LDXL01000010; KRT60406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZD03; -.
DR STRING; 1640512.XU09_C0010G0020; -.
DR PATRIC; fig|1640512.3.peg.1662; -.
DR Proteomes; UP000051388; 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 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; 2.
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 3: Inferred from homology;
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}.
FT REGION 579..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 483..510
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 552..579
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 579..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 66874 MW; 351A21537D060F9B CRC64;
MAKIIGIDLG TSNSAAAVMM GGKPTLIPAA EGTTIGGKAF PSYVAISKDG DLIVGEPARR
QAITNPDNTI VAAKRKMGTD HIFKLQGKEY KPQQISAFIL QKIKKDSEAF LGEKIEKAVI
TVPAYFDDNQ RQATKDAGTI AGLDVVRIIN EPTAASLAFG LDKSKQEMKI LVFDFGGGTL
DVTIMEMGGG VFEVMSTSGD TLLGGTDMDK VIIDYVVDDF RKKTGIDLTT DNTAMTRIRE
ASEKAKIELS TVMETDINLP FIFHDPSSGT KNLEIILTRA KFEELINPIV ERCKPSVEKA
LEDAKLPTSD ISKIVLIGGP TRIPLVRKFI SSLIGKEAES GVDPMEAVAM GAAIQAGIIA
GDITSDIVLL DVTPLTLGIE TLGGVREPLI ERNTTIPTSK SKVFTTAADS QTAVTIHVVQ
GERPMAADNV SLGSFNLTDL PPAPRGVPQI DVKFDIDANG ILNVTATDLG TKKEAKITIE
AGSKLSKDDI EKLKQDAEKF ADEDKKKKEA IDIKNEAESY IYTTEKLVNH DLKDKIPQEK
GIKITDAIRE LKEVLNKDAK QIKTKLDALK SLVNEVTTEL YKNVSPPHAD QQTGEDKQTG
GEQKSESTSD QGTTKENSSN
//
