ID A0A0G0S6T4_9BACT Unreviewed; 633 AA.
AC A0A0G0S6T4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 29.
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=UT50_C0008G0022 {ECO:0000313|EMBL:KKR21422.1};
OS Candidatus Moranbacteria bacterium GW2011_GWA2_39_41.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618695 {ECO:0000313|EMBL:KKR21422.1, ECO:0000313|Proteomes:UP000034867};
RN [1] {ECO:0000313|EMBL:KKR21422.1, ECO:0000313|Proteomes:UP000034867}
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:KKR21422.1}.
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; LBXA01000008; KKR21422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0S6T4; -.
DR PATRIC; fig|1618695.3.peg.344; -.
DR Proteomes; UP000034867; 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 REGION 596..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 633 AA; 68328 MW; 460BAE87C82F7B8C CRC64;
MGKVLGIDLG TTNSAMSVVE GGSPVIVENK EGVRTTPSMI AMSKTNERLV GLLAKRQAVT
NPENTLFSIK RLIGLHFNDP EVERDMKTMP YKIVKAGEGV KVLMGGKEYT PQEISAMVLA
KLKADAEEKL GQSITEAVIT VPAYFDDSQR KATIEAGEIA GLKVLRIINE PTAAALAYGF
NKKKDEKIAV YDLGGGTFDI SILEVSEDTV EVKSTNGDTH LGGDDFDQVL IHWIIDEFKK
QEGVDLSKDS LALQRIKESA EKAKIELSTA VETEINQPFI TADANGPKHL VMKLTRAKLE
ELVGELVQKT LEPTKKALAD AKLSVSDINE VILVGGMTRM PLVLQTVEKF FGKKPNISVN
PDEVVALGAA IQGGVLQGDV KDVLLLDVTP LTLGIETMGG VRTPLIDRNT TVPVNKSQTF
STAADNQPSV EIHILQGERE MAADNKTLGR FILDGIPPAP RGIPQVEVSF DIDANGILSV
KAKDKATGKE QSVRIEASTG LSKDEIERMK KDAEMHSEED KKKKELIEVR NLADTLTYST
EKALRDAGDK ITADEKKPVE DAIAELNKVK NSDDLSDIKA KTEALSQAAQ KIGEKLYKAA
QPEQPTPGAT EPASAEATGA AKEAETEKVA DSK
//
