ID   DNAK2_PROMM             Reviewed;         634 AA.
AC   Q7V3T5;
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 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=PMT_2255;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
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; BX548175; CAE22429.1; -; Genomic_DNA.
DR   RefSeq; WP_011131619.1; NC_005071.1.
DR   AlphaFoldDB; Q7V3T5; -.
DR   SMR; Q7V3T5; -.
DR   STRING; 74547.PMT_2255; -.
DR   PRIDE; Q7V3T5; -.
DR   EnsemblBacteria; CAE22429; CAE22429; PMT_2255.
DR   KEGG; pmt:PMT_2255; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_3; -.
DR   OMA; AYTKNQD; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001423; 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   Reference proteome; Stress response.
FT   CHAIN           1..634
FT                   /note="Chaperone protein dnaK2"
FT                   /id="PRO_0000078515"
FT   REGION          601..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   634 AA;  67763 MW;  2A43F0BCCCAA18F7 CRC64;
     MGKVVGIDLG TTNSCVAVME GGKPVVIANA EGFRTTPSVV AYTKNQDQLV GQIAKRQAVM
     NTDNTFYSAK RFVGRRVDEV NEESKEVSYE VEKSGSNVRL KCPVLDKQFS PEEVSAQVLR
     KLAEDAGKYL GENVTQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKSNERILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDKVI VDHLAATFKA
     NEGIDLRQDK QALQRLTEAA EKAKIELSSA TQSEINLPFI TATSEGPKHL DLTLTRAKFE
     ELASKLIDRC RVPVEQALKD AKLSSGELDE IVMVGGSSRM PAVQELVKRV TGKDPNQTVN
     PDEVVAVGAA IQGGVLAGEV KDILLLDVTP LSLGVETLGG VMTKMITRNT TVPTKKSETY
     STAVDGQTNV EIHVLQGERE MASDNKSLGT FRLDGIPPAP RGVPQIEVTF DIDANGILSV
     NAKDKGSGKE QSISITGAST LSENEVEKMV KDAETNASAD KEKRERIDIK NQAETLVYQA
     EKQLGELADK VDADSKAKVE DKRVKLKAAI EKDDFDAMKS LLEELQQELY TVGASVYQQA
     GAAAAESGAD AGAAGAGDSS SGDDVIDAEF TESK