ID   DNAK2_SYNE7             Reviewed;         634 AA.
AC   P50021; Q31KC1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 119.
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=Synpcc7942_2468;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8198610; DOI=10.1006/bbrc.1994.1724;
RA   Nimura K., Yoshikawa H., Takahashi H.;
RT   "Identification of dnaK multigene family in Synechococcus sp. PCC7942.";
RL   Biochem. Biophys. Res. Commun. 201:466-471(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; D28551; BAA05904.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58498.1; -; Genomic_DNA.
DR   PIR; JC2376; JC2376.
DR   RefSeq; WP_011378479.1; NC_007604.1.
DR   AlphaFoldDB; P50021; -.
DR   SMR; P50021; -.
DR   STRING; 1140.Synpcc7942_2468; -.
DR   PRIDE; P50021; -.
DR   EnsemblBacteria; ABB58498; ABB58498; Synpcc7942_2468.
DR   KEGG; syf:Synpcc7942_2468; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_3; -.
DR   OMA; AYTKNQD; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2468-MON; -.
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_0000078564"
FT   REGION          601..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        192
FT                   /note="D -> N (in Ref. 1; BAA05904)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   634 AA;  67768 MW;  4FFFA9D57C5E8E75 CRC64;
     MAKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AFAKNQDRLV GQIAKRQAVM
     NPENTFYSVK RFIGRRPDEV TNELTEVAYK VDTSGNAVKL DSSNAGKQFA PEEISAQVLR
     KLAEDASKYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKSNERILV FDLGGGTFDV SVLEVGDGVF EVLATSGDTH LGGDDFDKKI VDFLAGEFQK
     NEGIDLRKDK QALQRLTEAA EKAKIELSSA TQTEINLPFI TATQDGPKHL DLTLTRAKFE
     ELASDLIDRC RIPVEQAIKD AKLALSEIDE IVLVGGSTRI PAVQAIVKQM TGKEPNQSVN
     PDEVVAIGAA IQGGVLAGEV KDILLLDVTP LSLGVETLGG VMTKLIPRNT TIPTKKSETF
     STAADGQTNV EIHVLQGERE MASDNKSLGT FRLDGIPPAP RGVPQIEVIF DIDANGILNV
     TAKDKGSGKE QSISITGAST LSDNEVDRMV KDAEANAAAD KERRERIDLK NQADTLVYQS
     EKQLSELGDK ISADEKSKVE GFIQELKDAL AAEDYDKIKS IIEQLQQALY AAGSSVYQQA
     SAEASANAQA GPSSSSSSSS GDDDVIDAEF SESK