ID   DNAK1_PARMW             Reviewed;         662 AA.
AC   Q7U6R7;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=SYNW1269;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; BX569692; CAE07784.1; -; Genomic_DNA.
DR   RefSeq; WP_011128133.1; NC_005070.1.
DR   AlphaFoldDB; Q7U6R7; -.
DR   SMR; Q7U6R7; -.
DR   STRING; 84588.SYNW1269; -.
DR   PRIDE; Q7U6R7; -.
DR   EnsemblBacteria; CAE07784; CAE07784; SYNW1269.
DR   KEGG; syw:SYNW1269; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OMA; PCQSVNP; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001422; 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..662
FT                   /note="Chaperone protein dnaK1"
FT                   /id="PRO_0000078566"
FT   REGION          630..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   662 AA;  72512 MW;  ED67DE9B6E5789CB CRC64;
     MGRIVGIDLG TTNSVVAVLE AGRPHVIANA EGGRTTPSVV GYSKDQELLV GQLARRQLVL
     SPRNTFSNLK RFVGRDWEEL EDSSLAVPYT VRANDRGQVR VPCPVTEREY APEELVASII
     RKLVDDASTY LGESVEAAVV TVPAYFNDAQ RQATRDAGRL AGIAVERILN EPTAAALAYG
     FDRSAVRRVL VFDLGGGTFD VSLLRIANGV FDVKATNGDT QLGGNDFDQR IVDWIADAFQ
     AEHGVDLRRD RQALQRLTEA AEKAKQELSG VLTTPISLPF IATGENGPLH VETNLDRSTF
     EGLCPDLLDR LLMPVQSALR DSGWAADDID DVVLVGGATR MPMVQQLVRT LVPLDPCQSV
     NPDEVVAIGA AVQAGILTGE LRDLLLNDVT PLSLGLETVG GLMRVLIPRN TPIPVRQSDV
     FSTSEPNQSS VEIHVWQGER QMASDNKSLG RFRLSGIPPA PRGVPQVQVA FDIDANGLLQ
     VSATDRTTGR KQSVSIQGGS NLNEDEVTAL LAEAEARADE DRRKRNQIER RNRAQTLVAQ
     AERRLRDAAL ELGPYGAERQ QRAVEMAMRD VQDCLAQDDL QELDLCLSGL EEALFGLNRR
     LSAERQSDGR PLQGLRNTLG SLKDELFADD WDDDPWAAPS GPPRGRSLNR RDRDPWDDDF
     YR