ID   DNAK1_PROMA             Reviewed;         666 AA.
AC   Q7VC04;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=Pro_0938;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAP99982.1; -; Genomic_DNA.
DR   RefSeq; NP_875330.1; NC_005042.1.
DR   RefSeq; WP_011125090.1; NC_005042.1.
DR   AlphaFoldDB; Q7VC04; -.
DR   SMR; Q7VC04; -.
DR   STRING; 167539.Pro_0938; -.
DR   EnsemblBacteria; AAP99982; AAP99982; Pro_0938.
DR   GeneID; 54200281; -.
DR   KEGG; pma:Pro_0938; -.
DR   PATRIC; fig|167539.5.peg.987; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OMA; PCQSVNP; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001420; 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   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   Reference proteome; Stress response.
FT   CHAIN           1..666
FT                   /note="Chaperone protein dnaK1"
FT                   /id="PRO_0000078512"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   666 AA;  73309 MW;  AE4808E484DFD8AB CRC64;
     MGRIVGIDLG TTNSVIGVLE AGRPFVIANA EGSRTTPSVI GYTKESELVV GQQARRQLVL
     NPKNTFSNLK RYVGRSWDEL EENSLNVAYT IRANNQGCVR VTCPITEREY APEELIGSII
     RKLIDDAEKY LSETIDSAVI TVPAYFNDSQ RQATKDAALL AGVRVERILN EPTAAALAYG
     FDKSSSSRVL VFDLGGGTFD ISLLRISNGV FDVKATSGDT QLGGNDFDQK IVEWLANDFK
     KEHNIDLRRD RQSLQRLNEV AEKAKQELSG LNSTPISLPF IATGPNGPLH IETKLDRKTF
     ESLCKDLIDR LLQPVEVALQ DSGWTADDIN DVVLVGGGTR MPMVQQLVKT IVPVTPSQSV
     NPDEVVAIGA AVQAGILTGE LRDLLLNDVT PLSLGLETIG GLMKVLIPRN TPIPVRQADV
     FSTSEANQSS VEINVWQGER QLASDNKSLG KFRLSGIPPA PRGVPQVQVA FDIDANGMLQ
     VSATDRTTGR KQSVSINGGS NLNEDEVNNL IEEAKDKADV DRRKRASIDQ RNNALTLVAQ
     AERRLRDVSL EFGPYGAERQ QRAVEVSLRD VQDFLDSDDL AELDLAVSSL QEALFGLNRR
     ISAEKRTDNN PIQGIKNTFG SLKDELFSDD YWDDDPWDYH PNNNRVGGGR DYGGRNLDRW
     DNDFYN