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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//