ID   DNAK_BAUCH              Reviewed;         631 AA.
AC   Q1LST3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=BCI_0552;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA   Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT   sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF13904.1; -; Genomic_DNA.
DR   RefSeq; WP_011520714.1; NC_007984.1.
DR   AlphaFoldDB; Q1LST3; -.
DR   SMR; Q1LST3; -.
DR   STRING; 374463.BCI_0552; -.
DR   EnsemblBacteria; ABF13904; ABF13904; BCI_0552.
DR   KEGG; bci:BCI_0552; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002427; 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; 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..631
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059513"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   631 AA;  69030 MW;  292B0E375E158C4D CRC64;
     MGKIIGIDLG TTNSCIAIVE GTKTRVLENS EGDRTTPSIV AYTQDGEILV GQPAKRQSAT
     NPKNTLFAIK RLIGRRFEDE EVQRDVDIMP YKIIAADNGD AWLEIKGQKI APPQVSAEIL
     KKMKKTAEDY LGESVTEAVI TVPAYFNDTQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
     LDKEIGNRTI AVYDLGGGTF DISIIEIDDV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL
     VDEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSAAQQTD VNLPYITADS TGPKHMNLKI
     TRAKLESLVE DLVNRTMDPL KVALTDASLS ISDIKDVILV GGQTRMPLVQ KKVTDFFCKE
     PRKDVNPDEA VAIGAAVQGG VLSGNVKDVL LLDVTPLSLG IETMGGVMTA LIAKNTTIPT
     KHSQIFSTAE DNQSAVTIHV LQGERKRAMD NKSLGQFNLD GIAPAMRGIP QIEVTFDIDA
     DGILHVSAKD NNSGREQKIT IKASSGLSEE EIKKMVREAE ANAESDRKFE ELVQTRNQAD
     NLMHSTRKQL AEYGNQLLQE DRNAIENAIQ SLNTALKGES KTDIETNIQS LIQVSSKLLK
     LTQQQNQATN DNVKTDGNVV DAEFEEVKDK K