ID A0A1F3JP87_9BACT Unreviewed; 633 AA.
AC A0A1F3JP87;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=A2W98_07580 {ECO:0000313|EMBL:OFY18152.1};
OS Bacteroidetes bacterium GWF2_33_38.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797342 {ECO:0000313|EMBL:OFY18152.1, ECO:0000313|Proteomes:UP000177621};
RN [1] {ECO:0000313|EMBL:OFY18152.1, ECO:0000313|Proteomes:UP000177621}
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:OFY18152.1}.
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; MEOF01000062; OFY18152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3JP87; -.
DR STRING; 1797342.A2W98_07580; -.
DR Proteomes; UP000177621; 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 COMPBIAS 596..615
FT /note="Polar residues"
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; 69044 MW; 3DCCC4E479C6A6E3 CRC64;
MNKIIGIDLG TTNSCVSVME GNEPIVIPNS EGKRTTPSVV AFVDKGERKV GDPAKRQAIT
NPKKTISSIK RFMGEKFDKV AKEISRMPYE VVKGDNSTPR VKIDDRLYTP QEISAMILQK
MKKTAEDYLG HEVTEAVITV PAYFDDSQRQ ATKEAGEIAG LKVKRIINEP TAAALAYGMD
KKNKDIKVAV FDLGGGTFDI SILELGDGVF EVKSTNGDTH LGGDDFDQVI IDWLATEFKN
DENIDLRKDP MALQRLKEAA EKAKIELSSS TSTEINLPYI MPVDGVPKHL VRTLTRAKFE
QLSDSLIRAT IEPCKLAIKD AGVSVSDIDD VILVGGSTRI PAIQKIVEDF FKRTPSKGVN
PDEVVAIGAA IQGGVLTGEV TDVLLLDVTP LSLGIETMGG VMTKLIESNT TIPTKKAETF
TTAANNQPSV EIHVLQGERP IASGNKTIGR FHLDGIPPAP RGIPQVEVTF DIDANGILHV
SAKDKGTGKV QSIRIEASSG LTDDEINKMR DEAKANEAAD KQVKEKVDKL NSADSMIFQT
EKQIKDFGDK LPADKKEPIE KALANLKEAH KNQDVAAVDI AMEELNKVWQ VASEEMYKAS
SQEQQANSQG SPTEDTQTKK ENEVTDVDFE EVK
//
