ID A0A0G1N2E2_9BACT Unreviewed; 631 AA.
AC A0A0G1N2E2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=UW86_C0006G0012 {ECO:0000313|EMBL:KKT87237.1};
OS Microgenomates group bacterium GW2011_GWA1_Microgenomates_45_10.
OC Bacteria.
OX NCBI_TaxID=1618493 {ECO:0000313|EMBL:KKT87237.1, ECO:0000313|Proteomes:UP000034781};
RN [1] {ECO:0000313|EMBL:KKT87237.1, ECO:0000313|Proteomes:UP000034781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT87237.1}.
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DR EMBL; LCJY01000006; KKT87237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1N2E2; -.
DR PATRIC; fig|1618493.3.peg.209; -.
DR Proteomes; UP000034781; 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 508..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 631 AA; 67887 MW; 88EB5F35CD94B2AC CRC64;
MSKIIGIDLG TTNSCVAVME GGSPKVIHSA EGRNVIPSVV DPVTRVVGDV AKRQIVVKPK
ETIFSIKRLM GRRFKDESVQ YDLKWLPYAI KEGREGMAVV EVAGKSYTPQ EVSAMILQKI
KNDAESYLGE KVEKAVITVP AYFDDAQRQA TKQAGEIAGM EVVRIINEPT AAALAYGLDK
KQAHTIAVYD LGGGTFDISV LELGEGVYEV KSTNGDTHLG GDDFDKVILN FLAEEFKKEN
GIDLTKDPQA LQRLRDAAEK AKIELSTSTE AEVNLPFISQ GKEGPLHFVM KLTRSKLEVL
VGELITKTLE PVKKALTDAK VTAKEIDEVV LVGGMTRMPK VYEAVKSFFG REPNKSVNPD
EVVAVGAAVQ GAVLTGEIKD VVLLDVTPLT LAIETLGSVA TPMIPRNSTI PTSKTEVFST
AADNQTSVEV HVLQGERPMA TDNKSLGRFI LDGIPPAPRG MPQVEVTFDL DVNGILSVKA
KDKATSKEQS IRITGSTGLT KDEVEKMTKE AEAHAEEDQK RKTQTEARNQ ADGMIFTAEK
TLKDLGDKAP ADAKKGVEDK IAELKKDLDS ATVDQLKTKT EELSAALQKV GAAMYGQGQP
QAGPSAGSSE NPSTPPPSSE TDTVEEGKVV S
//
