ID A0A1F8NFM9_9CHLR Unreviewed; 629 AA.
AC A0A1F8NFM9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 25.
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=A2Z66_08195 {ECO:0000313|EMBL:OGO09668.1};
OS Chloroflexi bacterium RBG_13_66_10.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797637 {ECO:0000313|EMBL:OGO09668.1, ECO:0000313|Proteomes:UP000178877};
RN [1] {ECO:0000313|EMBL:OGO09668.1, ECO:0000313|Proteomes:UP000178877}
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:OGO09668.1}.
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DR EMBL; MGNE01000168; OGO09668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8NFM9; -.
DR Proteomes; UP000178877; 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.
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 511..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 629 AA; 68018 MW; BA0597BFBE0C40A9 CRC64;
MAKIVGIDLG TTNSVVAVME GGTPTVIPTA EGGRLCPSVV AFTKTGERMV GQTAKRQAVV
NSENTVYSIK RFMGRRFDEV ETERTMVSFE VFPGPSDDAR VRIPINNREY SPQEISAMIL
AKLKADAEAY LGEPVTKAVI TVPAYFNDSQ RQATKDAGKI AGFDVQRIIN EPTAAALAYG
LDKKENETIL VFDLGGGTFD VSLLEVGEGV TEVKSTNGDT HLGGDDWDQR IVNWAADEYK
KETGIDLRQD RQALQRLREA AEKGKIELSA VTETEINLPF ITADASGPKH MQMKLTRSKF
EQLTEDLVQR MRGPFEAVLR DAGMKASDVD EVVLVGGATR MPMAQDLVRS LTNKEPHKGV
NPDEVVAVGA AIQGGVLAGD VKDVLLVDVT PLSLGVETLG GVMTALIDRN TNIPIKKSEV
FSTADDGQTA VDIHVLQGER PMAGDNMTLG RFRLEGIPPA PRGVPQVEVT FDIDANGILN
VAARDRATGK EQKVTITAST NLSKAEVEKM VEEAKGHEAE DRKRRDLADA RNQGDSLAYQ
AEKSLRELGD KVPASDREKI EASLKSLREA LQGDDVPKIR QLTEQVQQAS YALGQQMYAQ
TQQPGPESGG PSEGPGSSGD VVEGEFRET
//
