ID   DNAK_PROM5              Reviewed;         634 AA.
AC   A2BZ91;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=P9515_18951;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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; CP000552; ABM73102.1; -; Genomic_DNA.
DR   RefSeq; WP_011821186.1; NC_008817.1.
DR   AlphaFoldDB; A2BZ91; -.
DR   SMR; A2BZ91; -.
DR   STRING; 167542.P9515_18951; -.
DR   PRIDE; A2BZ91; -.
DR   EnsemblBacteria; ABM73102; ABM73102; P9515_18951.
DR   KEGG; pmc:P9515_18951; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OMA; AYTKNQD; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001589; 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; 1.20.1270.10; -; 1.
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; IPR029048; HSP70_C_sf.
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; SSF100934; SSF100934; 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..634
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059629"
FT   REGION          592..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   634 AA;  68170 MW;  BBC3FD25298F8E49 CRC64;
     MGKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AYTKNQDQLV GQIAKRQAVM
     NPENTFYSAK RFVGRRVDEV NEESKDVSYG IEKAGSNVKL KCPVLDKQFS PEEVSAQVLR
     KLSEDAGKYL GENITQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKSNERILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDRCI VNHLASVFKS
     NEGIDLREDK QALQRLTEAA EKAKIELSNA TQSEINLPFI TATPDGPKHL DLNLTRANFE
     ELASKLIDRC RVPVEQALKD AKLSTGEIDE IVMVGGSTRM PAVQELVKRV TGKDPNQTVN
     PDEVVAVGAA IQGGVLAGEV KDILLLDVTP LSLGVETLGG VMTKMITRNT TVPTKKSETY
     STAVDGQTNV EIHVLQGERE MASDNKSLGT FRLDGIPSAP RGVPQIEVTF DIDANGILSV
     TAKDKGSGKE QSISITGAST LSDNEVDKMV KDAESNASVD KEKREKIDLK NQAETLVYQT
     EKQLGELGDK VDDSAKAKVE EKSKALKEAT SKEDYDSMKK LLEELQQELY AIGSSVYQQP
     GNQPPAPGGP NANASDDKGP DDDVIDADFT ETKD