ID A0A0G1YJK3_9BACT Unreviewed; 617 AA.
AC A0A0G1YJK3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=UY55_C0002G0185 {ECO:0000313|EMBL:KKW15127.1};
OS Candidatus Jorgensenbacteria bacterium GW2011_GWB1_50_10.
OC Bacteria; Candidatus Jorgensenbacteria.
OX NCBI_TaxID=1618665 {ECO:0000313|EMBL:KKW15127.1, ECO:0000313|Proteomes:UP000034224};
RN [1] {ECO:0000313|EMBL:KKW15127.1, ECO:0000313|Proteomes:UP000034224}
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:KKW15127.1}.
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DR EMBL; LCQK01000002; KKW15127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1YJK3; -.
DR STRING; 1618665.UY55_C0002G0185; -.
DR PATRIC; fig|1618665.3.peg.471; -.
DR Proteomes; UP000034224; 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 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 MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 617 AA; 66680 MW; 36A346D9EBCC6DFB CRC64;
MSKILGIDLG TTNSAMAVVE GGEPRVLESS EGNRTTPSIV AISKSNERLV GLLAKRQAVV
NPKNTIFSVK RLIGRKYSDK EVQEDKKWLS YELKGGEHGG VEIKMGERWY SPEEISAMVL
QKLKADAEAK LGEKIEEAVI TVPAYFDDSQ RQATKNAGEI AGFKVKRIIN EPTAAALAYH
LDRDKNERIV VYDFGGGTFD ISVLDVGEGT VEVKATGGDT HLGGDDFDKK IIEYLVAEYK
KQEGVDISSD SLAVQRLKEA AERAKHELST AMETEINLPY ITSDASGPKH FLMKLTRAKL
ENLVKDEIAR SIELVKETVT SPTPRGAGLK LSEINEVILV GGQTRMPAIQ EAVQKLFGKE
PHKGINPDEV VAVGAAVQAG IMQGDVKDVL LLDVTPLTFS IETLGGIATP MISKNTTVPT
AKTQVFSTAA DNQPSVEIHV GQGERPIMAD NKTLARFILD GLPPAPRGVP QIEVTFDIDA
NGILNVSAKD KASGKTQSVK IEASTSLNKE EIEKLKNEAA AHAAEDIKKK ELVETKNQAE
ALIYSSEKAL REAGDKVAAD IKDSVGKKID NLKNALKGDD VAQIKSALGE LTAEIQRVGE
ALYNVKKESD NEPPPSN
//
