ID A0A1G1PIM7_9BACT Unreviewed; 653 AA.
AC A0A1G1PIM7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 26.
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=A3F87_02810 {ECO:0000313|EMBL:OGX41782.1};
OS Omnitrophica WOR_2 bacterium RIFCSPLOWO2_12_FULL_51_24.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801869 {ECO:0000313|EMBL:OGX41782.1, ECO:0000313|Proteomes:UP000179359};
RN [1] {ECO:0000313|EMBL:OGX41782.1, ECO:0000313|Proteomes:UP000179359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGX41782.1}.
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DR EMBL; MHHC01000066; OGX41782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1PIM7; -.
DR STRING; 1801869.A3F87_02810; -.
DR Proteomes; UP000179359; 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 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; 2.
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 591..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 180
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 653 AA; 70637 MW; C1FF45E15A96000F CRC64;
MARAIGIDLG TSNSAAAVME GGHPVIIPSA EGAGVASGKA FPSYVAFTKD GQRLVGEPAR
RQAAINAEGT IQAAKRKMGT DYKFKVFGKE YTPQQISSFI LQKIKQDSEA YLGDKVEEAV
ITCPAYFDDN QRTATKDAGE IAGFKVLRVI NEPTAACLAY GLEKAGKEMK ILVFDFGGGT
LDVTIMEMWK EGGFKVMATS GDTQLGGTDM DNTLIDYIAN QFKRETGIDL KNDKMAMQRL
REGAEKAKVE LSSTLSTDIN LPFITADAAG PKHLTMSINR AKLEELVSPI IERCRGPLEQ
ALKDAKAAFE KENVSFAEKG VDKIIMVGGP TRMPIVQKFV EDYFGKKIER GVDPMECVAM
GAAIQAAIIK GEVKDVLLLD VTPLSLGIET LGGVNTKLID RNTTIPTRKS QVFSTAADNQ
TAVTIRVIQG ERPMADTEGN VELGRFDLVG IPAARRGVPQ IEVTFDIDAN GIVHVNAKDL
GTGKEQSIKI TAPKKLSKEE IDKMVKEAEK FASDDAKKKD EVEAVNQADN LVYTTEKSLK
DYGDKVSQQD RANIESMLND LKTAIKDKNL DRIKKSMEDL QQASYKLAEE IYKASSQKGP
AGPQGGQQPG GPQAGPEEPQ GGPEAGPESG PSKKDDIIDA DFRAEDDDDK KKK
//
