ID   DNAK_CHLT3              Reviewed;         637 AA.
AC   B3QZ38;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Ctha_1268;
OS   Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chloroherpeton.
OX   NCBI_TaxID=517418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35110 / GB-78;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL   Submitted (JUN-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; CP001100; ACF13731.1; -; Genomic_DNA.
DR   RefSeq; WP_012499815.1; NC_011026.1.
DR   AlphaFoldDB; B3QZ38; -.
DR   SMR; B3QZ38; -.
DR   STRING; 517418.Ctha_1268; -.
DR   PRIDE; B3QZ38; -.
DR   EnsemblBacteria; ACF13731; ACF13731; Ctha_1268.
DR   KEGG; cts:Ctha_1268; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001208; 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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119687"
FT   REGION          484..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..528
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   637 AA;  68541 MW;  77D0479D52F754AB CRC64;
     MGKIIGIDLG TTNSCVAVMQ GKDPVVIANA EGYRTTPSMV AFTKSGERLV GHAAKRQAIT
     NATNTIFSIK RFMGRTQDEV PEETKMVPYQ IVSEGNQARV KIGDKTHSPQ EISAMILQKM
     KETAEDFLGE KVTEAVITVP AYFNDAQRQA TKDAGQIAGL EVKRIINEPT AAALAYGLDK
     KQSNEKVAVF DLGGGTFDIS VLELGDGVFE VRSTDGDTHL GGDNFDQILI DFLADEFKKQ
     EMIDLRKDPM ALQRLKEAAE KAKIELSSSA ATEVNLPFIT ATQDGPKHLV VNITRAKFEG
     LCASLFDRIL EPCRRAVKNA KLDVKEIDEV VLVGGSTRIP KVQQLVKEFF GKEPNRSVNP
     DEVVAVGAAI QGGVLKGDVT DVLLLDVTPL SLGIETLGGV MTKLIEANTT IPTKKQETFS
     TAADNQTSVE IHILQGERPM STDNKTLGRF HLDGIPPAPR GVPQIEVAFD IDANGILHVS
     AKDKATGKEQ SVRIEASGKL SETEIEKMKK DASSHADEDK KKKEEVDTKN TADALIFSTE
     KQINEIGDKL PAENLSKIQA ALDRLKEAHK TGNTATIKPA MDALTKEWNE AASKMYGTEA
     GAPGAAGAAG AAGQGQSASS GKDDEVKNAD FEVVDDK