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Database: UniProt
Entry: A0A1F2RCP0_9BACT
LinkDB: A0A1F2RCP0_9BACT
Original site: A0A1F2RCP0_9BACT 
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
//
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