ID   DNAK_LEPCP              Reviewed;         646 AA.
AC   B1Y786;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Lcho_2576;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001013; ACB34841.1; -; Genomic_DNA.
DR   RefSeq; WP_012347597.1; NC_010524.1.
DR   AlphaFoldDB; B1Y786; -.
DR   SMR; B1Y786; -.
DR   STRING; 395495.Lcho_2576; -.
DR   EnsemblBacteria; ACB34841; ACB34841; Lcho_2576.
DR   KEGG; lch:Lcho_2576; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001693; 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..646
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119724"
FT   REGION          608..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   646 AA;  69606 MW;  7CE3E5197D727908 CRC64;
     MGKIIGIDLG TTNSCVAVME GNTTRVIENS EGARTTPSII AYQEDGEILV GASAKRQAVT
     NPRNTLYAVK RLIGRKFTEK EVQKDIDLMP YKIAAADNGD AWVEVRGKRM APPQVSAEVL
     RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
     LDKHGKGDRK IAVYDLGGGT FDISIIEIAD VDGEMQFEVL STNGDTFLGG EDFDQRIIDF
     IIAEFKKDQG VDLSKDVLAL QRLKEAAEKA KIELSNSAQT DINLPYITAD ASGPKHLNIK
     LTRAKLESLV EELIERTIAP CRTAMKDAGV SVGQIDDVIL VGGMSRMPKV QDKVKDFFGK
     EPRKDVNPDE AVAVGAAIQG QVLGGERKDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
     TKFSQTFSTA DDNQPAVTIK VYQGERELAS GNKSLGEFNL EGIPPSPRGT PQIEVTFDID
     ANGILHVGAK DKATGKENKI TIKANSGLSE DEIQKMVRDA EANAAEDKKK VEVVQAKNQG
     DAMVHSVKKS LTEYGDKLDA GEKEKIEAAM KDVEEAIKGD DKDDIEAKTN TLMTASQKLG
     EKMYADMQAQ QAAGAAAGPA GGEAPKSESK ADDADVVDAE FKEVKK