ID   DNAK_CHLMU              Reviewed;         655 AA.
AC   P56836;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=75 kDa membrane protein;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=TC_0675;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242.
RC   STRAIN=MoPn;
RX   PubMed=2254267; DOI=10.1128/jb.172.12.6959-6972.1990;
RA   Engel J.N., Pollack J., Perara E., Ganem D.;
RT   "Heat shock response of murine Chlamydia trachomatis.";
RL   J. Bacteriol. 172:6959-6972(1990).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Expressed early during infection.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE002160; AAF39496.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M62819; AAA23138.1; -; Genomic_DNA.
DR   PIR; H81676; H81676.
DR   RefSeq; WP_010231193.1; NZ_CP027217.1.
DR   AlphaFoldDB; P56836; -.
DR   SMR; P56836; -.
DR   STRING; 243161.TC_0675; -.
DR   PRIDE; P56836; -.
DR   EnsemblBacteria; AAF39496; AAF39496; TC_0675.
DR   GeneID; 1246036; -.
DR   KEGG; cmu:TC_0675; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000800; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..655
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078443"
FT   REGION          598..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         201
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        188
FT                   /note="G -> A (in Ref. 2; AAA23138)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   655 AA;  70572 MW;  E3C34698DABA1F53 CRC64;
     MSEKRKSNKI IGIDLGTTNS CVSVMEGGQP KVIASSEGTR TTPSIVAFKG SETLVGIPAK
     RQAVTNPEKT LASTKRFIGR KFSEVESEIK TVPYKVAPNS KGDAVFEVEN KLYTPEEIGA
     QILMKMKETA EAYLGETVTE AVITVPAYFN DSQRASTKDA GRIAGLDVKR IIPEPTAAAL
     AYGIDKEGDK KIAVFDLGGG TFDISILEIG DGVFEVLSTN GDTHLGGDDF DEVIINWMLG
     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 ASSGLKEEEI QQMIRDAELN KEEDKKRREA SDIKNEADGM
     IFRAEKAIKD YQDKIPADLV KEIEEQIEKV RQAVKEDAST TAIKAASDEL SARMQKIGEA
     MQAQSASAAN AQGGPNINSE DLKKHSFSTR PPAGDNSSST DNIEDADVEI VDKPE