ID   DNAK2_PROMP             Reviewed;         634 AA.
AC   Q7UZG3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Chaperone protein dnaK2;
DE   AltName: Full=HSP70-2;
DE   AltName: Full=Heat shock 70 kDa protein 2;
DE   AltName: Full=Heat shock protein 70-2;
GN   Name=dnaK2; OrderedLocusNames=PMM1704;
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; CAE20163.1; -; Genomic_DNA.
DR   RefSeq; WP_011133331.1; NC_005072.1.
DR   AlphaFoldDB; Q7UZG3; -.
DR   SMR; Q7UZG3; -.
DR   STRING; 59919.PMM1704; -.
DR   PRIDE; Q7UZG3; -.
DR   EnsemblBacteria; CAE20163; CAE20163; PMM1704.
DR   KEGG; pmm:PMM1704; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OMA; AYTKNQD; -.
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; 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 dnaK2"
FT                   /id="PRO_0000078517"
FT   REGION          592..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..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:0000250"
SQ   SEQUENCE   634 AA;  68244 MW;  032E44A472D89647 CRC64;
     MGKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AYTKNQDQLV GQIAKRQAVM
     NPENTFYSAK RFVGRRVDEV NEESKEVSYG IEKAGSNVKL KCPVLDKQFS PEEVSAQVLR
     KLSEDAGKYL GENITQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKSNERILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDRCI VDHLASIFKS
     NEGIDLRQDK QALQRLTEAA EKAKIELSNA TQSEINLPFI TATPEGPKHL 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 VDASAKAKVE EKSKALKEAT SKEDYEAMKK LLEELQQELY AIGSSVYQQP
     GNQPPAPGTP DSNESNDKGG DDDVIDADFT ETKD