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Database: UniProt
Entry: A0A0G1YEQ7_9BACT
LinkDB: A0A0G1YEQ7_9BACT
Original site: A0A0G1YEQ7_9BACT 
ID   A0A0G1YEQ7_9BACT        Unreviewed;       634 AA.
AC   A0A0G1YEQ7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 27.
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=UY90_C0048G0008 {ECO:0000313|EMBL:KKW41655.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWA2_54_9.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619059 {ECO:0000313|EMBL:KKW41655.1, ECO:0000313|Proteomes:UP000034940};
RN   [1] {ECO:0000313|EMBL:KKW41655.1, ECO:0000313|Proteomes:UP000034940}
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:KKW41655.1}.
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DR   EMBL; LCRV01000048; KKW41655.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1YEQ7; -.
DR   PATRIC; fig|1619059.3.peg.748; -.
DR   Proteomes; UP000034940; 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          603..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          244..271
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         195
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   634 AA;  69091 MW;  20C2B8F845345612 CRC64;
     MSKVIGIDLG TTNSCVAVIE GGEPVVIPNA EGNRTTPSVV AFKNDEILTG IAAKRQAVTN
     PENTIYSSKR FVGRRFSEVR KEAEHMPFTV KEGKEGRAVI VVQGKEMLPQ EISAKVLQKL
     KKDAEAYLGT TVDKAVITVP AYFDDSQRQA TKNAGEIAGL EVLRIINEPT AASLAYGLDK
     GHEHKIAVYD LGGGTFDVSI LELAEGVFEV LSTNGDTHLG GDDFDQVIIE WILSEFKKDQ
     GVDLSKDRIA LQRLKEAAEK AKIELSSQNE TDINLPFITA DNTGPKHLNL KLSRAKLEAL
     VADLIEKTVK PCELALKDAG LTKSGIDEVV LVGGMTRMPA VQAKVKKLFG REPHKGVNPD
     EVVAIGAAIQ AGVMGGDIDR DIVLVDVTPL SLGIETLGGV ATKLIERNTK IPTNKSQIFS
     TAADNQPSVE VHIVQGEREM ASDNKSLGRF ILDGIATAPR GIPQIEVSFD IDTNGILNVK
     AKDKGTGKEQ HITIQGSTGL SDEEIEKMKK DAEMHAEEDR KKKGKVDARN NTDALIFNLE
     KQMREYDAKI TDSVKKKVNE KMNIVKDLLK KEDTSAEELK KATEELATEA QEIGKIIYEE
     AQKAEQKGGA EKKGKDNIVD AEVVDEKEEK RKKK
//
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