ID A0A1F2RCP0_9BACT Unreviewed; 637 AA.
AC A0A1F2RCP0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, 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=A3H95_08850 {ECO:0000313|EMBL:OFV94457.1};
OS Acidobacteria bacterium RIFCSPLOWO2_02_FULL_64_15.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1797181 {ECO:0000313|EMBL:OFV94457.1, ECO:0000313|Proteomes:UP000179236};
RN [1] {ECO:0000313|EMBL:OFV94457.1, ECO:0000313|Proteomes:UP000179236}
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:OFV94457.1}.
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DR EMBL; MEKS01000003; OFV94457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2RCP0; -.
DR STRING; 1797181.A3H95_08850; -.
DR Proteomes; UP000179236; 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; 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 590..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Basic and acidic 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 637 AA; 67886 MW; B4CD888DC3B97DE0 CRC64;
MPAKVIGIDL GTTNSVVAVM EGGEPTVIVN QEGARLTPSV VAMAKNGERL VGQVARRQAV
TNPENTVFSI KRFMGRKFEE VSSEATRVPY KVARASNGDA WVEVRGKASS PPEISAMVLQ
KLKQAAEDYL GEKVTDAVIT VPAYFNDAQR QATKDAGKIA GLNVLRIINE PTAAALAYGL
DKKKDETIAV YDFGGGTFDI SVLEVGEGVV EVKATNGDTH LGGDDLDDRI IEWLAAEFKK
TEGIDLAKDR MALQRLKEGA EKAKIELSTA METEINLPFV TADQSGPKHL QVKLSRAKLE
QLVDDLLQRT MGPVKQALAD AGVDPKKIDE VVLVGGSTRM PKVQQLVRDY FGKDPHKGVN
PDEVVAVGAA VQGGVLTGDV KDMLLLDVTP LSLGIETLGG VMTTLIARNT TIPTRKSETF
STAADNQTSV EVHVLQGERP LARDNRTLGR FHLIGLPPAP RGVPQVEVSF DIDANGIVNV
AAKDLGTGKE QKITITASSG LAKEEVDRMV KDAQSHAAED QARRDLIEAR NQADSLAYQV
EKTVNDNREK VPVGELSRIE SAIADARKAA QGDDLTAIRK AMDELQRVSH SLAEQLDKGS
GGSSGTSGSG GSGGARGSEG SGVKEGEVVD AEYAETR
//