ID Q062E4_9SYNE Unreviewed; 639 AA.
AC Q062E4;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
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 ECO:0000313|EMBL:EAU71208.1};
GN ORFNames=BL107_06744 {ECO:0000313|EMBL:EAU71208.1};
OS Synechococcus sp. BL107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=313625 {ECO:0000313|EMBL:EAU71208.1, ECO:0000313|Proteomes:UP000004390};
RN [1] {ECO:0000313|EMBL:EAU71208.1, ECO:0000313|Proteomes:UP000004390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL107 {ECO:0000313|EMBL:EAU71208.1,
RC ECO:0000313|Proteomes:UP000004390};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC 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:EAU71208.1}.
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DR EMBL; AATZ01000002; EAU71208.1; -; Genomic_DNA.
DR RefSeq; WP_009788574.1; NZ_DS022298.1.
DR AlphaFoldDB; Q062E4; -.
DR STRING; 313625.BL107_06744; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000004390; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 601..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..273
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 639 AA; 68200 MW; C104BF4AC6DCDA45 CRC64;
MGKVVGIDLG TTNSCVSVME GGKPTVIANA EGFRTTPSVV AYTKNQDQLV GQIAKRQAVM
NPDNTFYSVK RFIGRRVDEV SEEQKEVSYG VEKSGSNVKV KCPVLDKQFA PEEVSAQVLR
KLAEDAGKYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
DKKSNERILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDKVI VDHLAATFKS
NEGIDLRQDK QALQRLTEAA EKAKIELSNA TQSEINLPFI TATPEGPKHL DLTLTRAKFE
ELASNLIDRC RVPVEQALKD AKLSSGELDE IVMVGGSTRI PAVLDLVKRT TSKDPNQTVN
PDEVVAVGAA IQGGVLAGEV KDILLLDVTP LSLGVETLGG VMTKMITRNT TVPTKKSETY
STAVDGQTNV EIHVLQGERE MASDNKSLGT FRLDGIPPAP RGVPQIEVTF DIDANGILSV
TAKDKGSGKE QSISITGAST LSDSEVDKMV KDAETNASAD KEKRERIDLK NQAETLVYQA
EKQMTELADK VDADAKAKVE EKRVKLKDAV EAEDYDAMKT LLEELQQELY TVGASVYQQD
GAQAGGAAPD GDAAADANGG AGGGNAADDV IDAEFTETK
//
