ID A0A1F6R7A6_9BACT Unreviewed; 632 AA.
AC A0A1F6R7A6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 24.
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=A3J63_01460 {ECO:0000313|EMBL:OGI16498.1};
OS Candidatus Moranbacteria bacterium RIFCSPHIGHO2_02_FULL_40_12b.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1801639 {ECO:0000313|EMBL:OGI16498.1, ECO:0000313|Proteomes:UP000176579};
RN [1] {ECO:0000313|EMBL:OGI16498.1, ECO:0000313|Proteomes:UP000176579}
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:OGI16498.1}.
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DR EMBL; MFRX01000041; OGI16498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6R7A6; -.
DR STRING; 1801639.A3J63_01460; -.
DR Proteomes; UP000176579; 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..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..632
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 632 AA; 68671 MW; 2985042CCF5B7FE1 CRC64;
MSKILGIDLG TTNSAMAVIE AGKPTIVENK EGARTTPSMV AISKGNERLV GLLAKRQAVT
NPGNTLFSIK RLIGRHFSAD EVQKDVKTLP YKIKQAGEGV VVEMGGRDYT PQEISAMILG
KLKADAEEKL GEKITEAVIT VPAYFDDSQR KATKEAGEIA GFSVKRIINE PTAAALAYGF
NKKKEEKIAV YDLGGGTYDI SILEIGDDTV EVKSTNGDTH LGGDDFDQVI IHWIISEFKK
QEGIDLSKDP LALQRIKEAA EKAKIELSTA METEINQPFI TSDSSGPKHM VMKMTRAKLE
ELVGDLVEKT LEPMKKALTD AKMETKDINE VIMVGGMTRM PLVLQTVEKF FGKKTNITVN
PDEVVALGAA IQGGVLQGDV KDVLLLDVTP LTLGIETLGG VRTALINRNT TVPTMKSQIF
STAADNQPSV EIHVLQGERE MAADNKTLGR FILDGIPPSP RGIPQVEVTF DIDANGILSV
KAKDKATNKE QSIRIEASTG LSKDEIEKMK KDADLHAEED KKKKELVEAR NMADTLSYTT
EKALRDAGDK ITADEKKPVE DAVAELNKVK NGDDLEAIKK ATEVLSQSAQ KIGEKLYKAA
QSASSADKEP PKEEGPKDAE VEDDKKDEGE KK
//
