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Database: UniProt
Entry: K2EXG4_9BACT
LinkDB: K2EXG4_9BACT
Original site: K2EXG4_9BACT 
ID   K2EXG4_9BACT            Unreviewed;       470 AA.
AC   K2EXG4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 34.
DE   RecName: Full=Molecular chaperone DnaK {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=ACD_12C00674G0001 {ECO:0000313|EMBL:EKE14092.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE14092.1};
RN   [1] {ECO:0000313|EMBL:EKE14092.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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:EKE14092.1}.
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DR   EMBL; AMFJ01005067; EKE14092.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2EXG4; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
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; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   NON_TER         470
FT                   /evidence="ECO:0000313|EMBL:EKE14092.1"
SQ   SEQUENCE   470 AA;  51073 MW;  5EE4282D62C1774D CRC64;
     MAKIIGIDLG TTNSCVAVME GGKPKVIFSQ EGRNTIPSVV DPVKRIVGDV AKRQMVVNPK
     NTVFSIKRLV GRRFTDESVK FDAKWLPYKI VQGRDEMADV EIEGKTYTPQ EISAMILQKI
     KTDAEAHLGE KVDKAVITVP AYFDDAQRQA TKQAGEIAGL EVVRIINEPT AAALAYGLDK
     KHSHTIAVYD LGGGTFDITV LELGEGVFEV KATNGDTHLG GDDFDKVILD YIADEFKKDN
     GVDLRKDPQA LQRLRDAAEK AKIELSTSKE AEVNLPFVTV KDGQPSHLVM KIGRNKLESL
     VGDLIEKTFG PVKAVLKDAK VEVSKIDEVV LVGGMTRMPK VIEKVKEFFG KEPNRSVNPD
     EVVALGAAIQ GGVLTGETKD VVLLDVTPLT LGLETLGGVM TPLIQKNTTV PNTKAEVFST
     AGDNQTQVEI HIMQGERPLA RDNKSLGRFT LDGIPPAPRG VPQIEVSFDL
//
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