ID A0A0P9EKY6_9ARCH Unreviewed; 642 AA.
AC A0A0P9EKY6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Molecular chaperone DnaK {ECO:0000313|EMBL:KPV63545.1};
GN ORFNames=AOA66_0822 {ECO:0000313|EMBL:KPV63545.1};
OS Candidatus Bathyarchaeota archaeon BA2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV63545.1, ECO:0000313|Proteomes:UP000050284};
RN [1] {ECO:0000313|EMBL:KPV63545.1, ECO:0000313|Proteomes:UP000050284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA2 {ECO:0000313|EMBL:KPV63545.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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:KPV63545.1}.
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DR EMBL; LIHK01000021; KPV63545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9EKY6; -.
DR STRING; 1700836.AOA66_0822; -.
DR KEGG; barb:AOA66_0822; -.
DR PATRIC; fig|1700836.3.peg.1423; -.
DR Proteomes; UP000050284; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
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 InterPro; IPR000048; IQ_motif_EF-hand-BS.
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; PS01036; HSP70_3; 1.
DR PROSITE; PS50096; IQ; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322}.
SQ SEQUENCE 642 AA; 71881 MW; E2D92C7982C5D7A8 CRC64;
MGRTIGIDLG TTNSAGAVMK YGKIRLVPAS EGPIPYGKMF PSIVAFKEDG EIIVGKNAKD
YAYVHPDRTI RWIKRKMGTD YTVDIDGRKY TPQEISALIL KKIKRDAEIY LGEKIDKAVI
SAPAYFNNNQ RNATREAGEI AGLEVLRIVS EPTAASLAYG LDKIRKNLKI AVLDLGAGTF
DVTILQMNNG IFKVISISGD THLGGKDMDD RILNYLVDKI EEKYGINLRD DQKNLNKLRD
AGEMAKIHLS SKLSTTIKTQ LNIDGSNINP HIVLTRDKLE ELIKPELDRL RDPLEQALKD
AGLEPQDIDK LVFVGGPTRM PVIRRYFKDF FSGLESEEGI DPMGIVAVGA SIQASVLKGE
IRDMLLLDVT PLSLGVETSG GVFTRLIKRN TTIPTEESMI FVTEEEDQTS MMIHVLQGER
EMAKDNISLG LFKLDGIPPA PRYEQEVEVT FQIDADGILN VSTEILETGK KEAIKVTKPT
ELSEEEITRM IIEATKFDKV DKRKKEIVET CNRAEAVIYA TEKSIEEMCR KISEGEKRKL
EETLGKLKTA LNGDNTQKIQ GYTDELLELV KGANMKVKKI SQAKRLVSSV EKRLRGKVSR
EERRKVEEAV KRLEGTPYKD VGKEMNKLKE MIILLEADYG ER
//