ID   DNAK_PARUW              Reviewed;         654 AA.
AC   Q6MB26;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=pc1499;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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; BX908798; CAF24223.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6MB26; -.
DR   SMR; Q6MB26; -.
DR   STRING; 264201.pc1499; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000529; 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..654
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225989"
FT   REGION          592..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..654
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         205
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   654 AA;  71371 MW;  5ADF97C69E630E1B CRC64;
     MTMSQSQTKK GRIIGIDLGT TNSCVAVMEG GAPKVIASAE GTRTTPSVVA YKGNERLVGI
     PAKRQAVTNP ENTITSSKRF IGRKYQEVLS EIKTVPYKVT NNNNGDAVFE IQGKIVTPEE
     IAAQILIKMK ETAEAYLGEK ITEAVITVPA YFNDSQRQST KDAGRIAGLD VKRIIPEPTA
     AALAYGLDKE NADKKIAVFD LGGGTFDISV LEIGDGVFEV LSTSGDTHLG GDDFDNAILN
     WMLETFKQEQ GIDLRNDKMA LQRLRDAAEK AKIELSGVQQ TEINQPFITM DASGPKHLTM
     TLTRSKLESL THDLIERTRE PCLKALKDSG LNKDDISEVI LVGGMSRMPA VQEVVKSIFG
     KEGHKGVNPD EVVAVGAAIQ GGVLTGVVKD VLLLDVTPLT LGIETLGGVM TPLVERNTTI
     PTQKKQIFST AADNQPAVTI RVLQGERKMA NDNKEIGRFD LADIPPSPRG TPQIEVAFDI
     DADGILHVSA KDLSSGKEQK IRIEAQSGLQ EEEIKRMVRD AEEHAEEDKK RKEEVEIRNE
     ADSLAFRAQK ALDEYKDKVP QQIADDISNK IEAVKKALET TDIARIRSAK DELERQMQQI
     GEVMSKAAGQ SETQSTGPGS YQESSNQSSQ HQTNNNKPDD IEEAEVEILD DKKP