ID   DNAK1_SYNE7             Reviewed;         655 AA.
AC   P50020; Q31LG6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Chaperone protein dnaK1;
DE   AltName: Full=HSP70-1;
DE   AltName: Full=Heat shock 70 kDa protein 1;
DE   AltName: Full=Heat shock protein 70-1;
GN   Name=dnaK1; OrderedLocusNames=Synpcc7942_2073;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8198610; DOI=10.1006/bbrc.1994.1724;
RA   Nimura K., Yoshikawa H., Takahashi H.;
RT   "Identification of dnaK multigene family in Synechococcus sp. PCC7942.";
RL   Biochem. Biophys. Res. Commun. 201:466-471(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; D28550; BAA05903.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58103.1; -; Genomic_DNA.
DR   PIR; JC2238; JC2238.
DR   RefSeq; WP_011378303.1; NC_007604.1.
DR   AlphaFoldDB; P50020; -.
DR   SMR; P50020; -.
DR   STRING; 1140.Synpcc7942_2073; -.
DR   PRIDE; P50020; -.
DR   EnsemblBacteria; ABB58103; ABB58103; Synpcc7942_2073.
DR   KEGG; syf:Synpcc7942_2073; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2073-MON; -.
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   GO; GO:0051301; P:cell division; 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   InterPro; IPR003494; SHS2_FtsA.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SMART; SM00842; FtsA; 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 dnaK1"
FT                   /id="PRO_0000078563"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        107
FT                   /note="V -> F (in Ref. 1; BAA05903)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476
FT                   /note="D -> G (in Ref. 1; BAA05903)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        508
FT                   /note="S -> G (in Ref. 1; BAA05903)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   655 AA;  71098 MW;  52202216EA3C75BF CRC64;
     MGKVIGIDLG TTNSCVAVLE GGKPIIVTNR EGDRTTPSIV AVGRKGDRIV GRMAKRQAVT
     NAENTVYSIK RFIGRRWEDT EAERSRVTYT CVPGKDDTVN VTIRDRVCTP QEISAMVLQK
     LRQDAETFLG EPVTQAVITV PAYFTDAQRQ ATKDAGAIAG LEVLRIVNEP TAAALSYGLD
     KLHENSRILV FDLGGSTLDV 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