ID   A0A1H3GVZ0_9EURY        Unreviewed;       647 AA.
AC   A0A1H3GVZ0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=SAMN05216564_10312 {ECO:0000313|EMBL:SDY07210.1};
OS   Halopenitus persicus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halopenitus.
OX   NCBI_TaxID=1048396 {ECO:0000313|EMBL:SDY07210.1, ECO:0000313|Proteomes:UP000199079};
RN   [1] {ECO:0000313|EMBL:SDY07210.1, ECO:0000313|Proteomes:UP000199079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC30,IBRC 10041,KCTC 4046 {ECO:0000313|Proteomes:UP000199079};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNPC01000003; SDY07210.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3GVZ0; -.
DR   OrthoDB; 9944at2157; -.
DR   Proteomes; UP000199079; 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   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          489..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          226..253
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        495..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..647
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   647 AA;  68921 MW;  C6DC0D6A178FF23B CRC64;
     MASNKILGID LGTTNSAFAV MEGGDPEIIA NAEGDRTTPS IVAFSDDGER LVGKPAKNQA
     VQNPDRTIQS IKRHMGEEDY TVAIEDEEYT PEQVSAMILQ KIKRDAEEYL GDEIEKAVIT
     VPAYFNDKQR QATKDAGEIA GFEVDRIVNE PTAAAMAYGL DDESDQTVLV YDLGGGTFDV
     SILDLGGGVY EVVATNGDND LGGDDWDEAI IDHLAEEFEN DHGIDLREDR QALQRLTEAA
     EEAKIELSNK KETTVNLPFI TATDSGPVHL EQSITRATFE SLTEDLLERT VGPTEQALED
     AGYAKDDIDE VILVGGSTRM PQVQEKVEEL VGQEPKKNVN PDEAVALGAA VQGGVLSGDV
     DDIVLLDVTP LSLGIEVKGG LFERLIEKNT TIPTEASKVF TTAADNQTSV NVRVFQGERE
     IAEENELLGA FQLTGIPPAP AGTPQIEVSF NIDENGIVNV EAEDQGSGNA ESITIEGGAG
     LSDEEIEQMQ EEAEQHAEED EKRRERIEAR NEAESTVQRA ETLIEENEEN VDDDVIAEIE
     AAMDDVEDVL ADEDADIDEI ESATEDLADQ LQEIGKQMYQ EQAAQAGAAG GAGAAGAGPG
     GMGGAGPGGM GGAGPGGAAG NGAGEPGDDE YVDADFEDVD DENEDEE
//