ID   DNAK1_PROMP             Reviewed;         665 AA.
AC   Q7V1H4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=PMM0897;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(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; BX548174; CAE19356.1; -; Genomic_DNA.
DR   RefSeq; WP_011132530.1; NC_005072.1.
DR   AlphaFoldDB; Q7V1H4; -.
DR   SMR; Q7V1H4; -.
DR   STRING; 59919.PMM0897; -.
DR   EnsemblBacteria; CAE19356; CAE19356; PMM0897.
DR   KEGG; pmm:PMM0897; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_0_3; -.
DR   OMA; PCQSVNP; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001026; 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   Stress response.
FT   CHAIN           1..665
FT                   /note="Chaperone protein dnaK1"
FT                   /id="PRO_0000078516"
FT   REGION          634..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..665
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   665 AA;  73430 MW;  F530437A77BC6B86 CRC64;
     MGQIVGIDLG TTNSVVGVIE AGRPVVIANS EGTRTTPSIV GFTKNSEIVI GDQARRQLVL
     NPKNTFYNLK RFIGRDWDEL DETSISVPYN VKSNDKGSVR ILSPFTEREY APEELISSII
     RKLINDAETY LGDTIDSAVI TVPAYFNESQ RQATKDSAVL AGIKVDRILN EPTAAALAYG
     FEKSSSNNVL VFDLGGGTFD VSLLRISNGV FDVKATCGDT QLGGNNFDSK IVDWIAERFL
     EKHKIDLRRD RQALQRLTEA AEKAKCELSG LQKTKISLPF ITTSDDGPLH IEEEFDRKLF
     ESLSDDLLDR LLEPVQIALE DSGWDAEQID EVVLVGGSTR IPMVQQLVKT LVPNEPCQSV
     NPDEVVAIGA AIQSGIISGD LRDLLLNDVT PLSLGLETIG GLMKVLIPRN TPIPVRQSDV
     FSTSESNQSS VVVQVRQGER PLASENKSLG KFRLSGIPPA PRGIPQVQVA FDIDANGLLE
     VSATDRTTGR KQTVSISGGS NLNEQEINMM IAEAKSKSTE DRIKRSVIDR KNNALTLIAQ
     AERRLRDASL EFGPYGAERQ QRAVELAIQD VEEFIDDDDP QELEISVSSL QEALFGLNRR
     FAAEKKVDSN PLQGIKNTFG SLKDELFSDD YWDDDPWDNQ MNSNSRNSRY GNSRDDDPWD
     NDYFL