ID   DNAK_CHLT2              Reviewed;         660 AA.
AC   B0B7W6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=CTL0652;
OS   Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=434/Bu / ATCC VR-902B;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
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; AM884176; CAP04092.1; -; Genomic_DNA.
DR   RefSeq; WP_009872626.1; NC_010287.1.
DR   RefSeq; YP_001654725.1; NC_010287.1.
DR   AlphaFoldDB; B0B7W6; -.
DR   SMR; B0B7W6; -.
DR   EnsemblBacteria; CAP04092; CAP04092; CTL0652.
DR   KEGG; ctb:CTL0652; -.
DR   PATRIC; fig|471472.4.peg.702; -.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000795; 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   Stress response.
FT   CHAIN           1..660
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205178"
FT   REGION          599..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         201
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   660 AA;  70843 MW;  C189001C9197EAE4 CRC64;
     MSEKRKSNKI IGIDLGTTNS CVSVMEGGQP KVIASSEGTR TTPSIVAFKG GETLVGIPAK
     RQAVTNPEKT LASTKRFIGR KFSEVESEIK TVPYKVAPNS KGDAVFDVEQ KLYTPEEIGA
     QILMKMKETA EAYLGETVTE AVITVPAYFN DSQRASTKDA GRIAGLDVKR IIPEPTAAAL
     AYGIDKEGDK KIAVFDLGGG TFDISILEIG DGVFEVLSTN GDTHLGGDDF DGVIINWMLD
     EFKKQEGIDL SKDNMALQRL KDAAEKAKIE LSGVSSTEIN QPFITIDANG PKHLALTLTR
     AQFEHLASSL IERTKQPCAQ ALKDAKLSAS DIDDVLLVGG MSRMPAVQAV VKEIFGKEPN
     KGVNPDEVVA IGAAIQGGVL GGEVKDVLLL DVIPLSLGIE TLGGVMTPLV ERNTTIPTQK
     KQIFSTAADN QPAVTIVVLQ GERPMAKDNK EIGRFDLTDI PPAPRGHPQI EVTFDIDANG
     ILHVSAKDAA SGREQKIRIE ASSGLKEDEI QQMIRDAELH KEEDKQRKEA SDVKNEADGM
     IFRAEKAVKD YHDKIPAELV KEIEEHIEKV RQAIKEDAST TAIKAASDEL STRMQKIGEA
     MQAQSASAAA SSAANAQGGP NINSEDLKKH SFSTRPPAGG SASSTDNIED ADVEIVDKPE