ID   DNAK3_SYNP6             Reviewed;         655 AA.
AC   Q5N0G0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Chaperone protein DnaK 3 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 3 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein 3 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 3 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK3 {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=syc2020_c;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; AP008231; BAD80210.1; -; Genomic_DNA.
DR   RefSeq; WP_011244330.1; NC_006576.1.
DR   AlphaFoldDB; Q5N0G0; -.
DR   SMR; Q5N0G0; -.
DR   STRING; 269084.syc2020_c; -.
DR   EnsemblBacteria; BAD80210; BAD80210; syc2020_c.
DR   KEGG; syc:syc2020_c; -.
DR   eggNOG; COG0443; Bacteria.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001175; Chromosome.
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   Gene3D; 2.60.34.10; -; 1.
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; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..655
FT                   /note="Chaperone protein DnaK 3"
FT                   /id="PRO_0000226020"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   655 AA;  71067 MW;  9105D1E21A5C8866 CRC64;
     MGKVIGIDLG TTNSCVAVLE GGKPIIVTNR EGDRTTPSIV AVGRKGDRIV GRMAKRQAVT
     NAENTVYSIK RFIGRRWEDT EAERSRVTYT CVPGKDDTVN VTIRDRVCTP QEISAMVLQK
     LRQDAETFLG EPVTQAVITV PAYFTDAQRQ ATKDAGAIAG LKVLRIVNEP TAAALSYGLD
     KLHENSRILV FDLGGGTLDV SILQLGDSVF EVKATAGNNH LGGDDFDAVI VDWLADNFLK
     AESIDLRQDK MAIQRLREAS EQAKIDLSTL PTTTINLPFI ATATVDGAPE PKHIEVELQR
     EQFEVLASNL VQATIEPIQQ ALKDSNLTID QIDRILLVGG SSRIPAIQQA VQKFFGGKTP
     DLTINPDEAI ALGAAIQAGV LGGEVKDVLL LDVIPLSLGL ETLGGVFTKI IERNTTIPTS
     RTQVFTTATD GQVMVEVHVL QGERALVKDN KSLGRFQLTG IPPAPRGVPQ IELAFDIDAD
     GILNVSARDR GTGRAQGIRI TSTGGLTSDE IEAMRRDAEL YQEADQINLQ MIELRTQFEN
     LRYSFESTLQ NNRELLTAEQ QEPLEASLNA LASGLESVSN EAELNQLRQQ LEALKQQLYA
     IGAAAYRQDG SVTTIPVQPT FADLIGDNDN GSNETVAIER NDDDATVTAD YEAIE