ID   DNAK_MYCPU              Reviewed;         599 AA.
AC   Q98QY7;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=MYPU_2230;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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; AL445563; CAC13396.1; -; Genomic_DNA.
DR   PIR; G90539; G90539.
DR   RefSeq; WP_010925027.1; NC_002771.1.
DR   AlphaFoldDB; Q98QY7; -.
DR   SMR; Q98QY7; -.
DR   STRING; 272635.MYPU_2230; -.
DR   PRIDE; Q98QY7; -.
DR   EnsemblBacteria; CAC13396; CAC13396; CAC13396.
DR   KEGG; mpu:MYPU_2230; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_14; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; MPUL272635:G1GT6-222-MON; -.
DR   Proteomes; UP000000528; 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; 2.
DR   Pfam; PF00012; HSP70; 2.
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..599
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078497"
FT   REGION          575..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         187
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   599 AA;  65521 MW;  43CAFCAA7FAA9294 CRC64;
     MAKEIILGID LGTTNSVVSI IENKKPVVLE NFNGKRTTPS VVAFKNGEIQ VGEIAKRQLE
     TNPDTIASIK RLMGTTKTVK ANGKTYKPEE ISAMILSHLK EYAEKKVGKK LTKAVITVPA
     YFDNSQREAT KIAGKIAGLD VLRIINEPTA AALSFGLDKK EKEMKVLVYD LGGGTFDVSV
     LELENGTFEV LSTSGDNHLG GDDWDHVIVE WLTKEIKNRY DFDPSKDKMV MTRLKEAAEK
     AKIDLSAQMV AQITLPFLSV TSKGPINVDL ELKRSEFEKM TTHLVDRTRK PIEDALREAK
     IKASDLSEVL LVGGSTRIPA VQSMVEHVLG KKPNRSINPD EVVAIGAAIQ GGVLAGDIND
     VLLLDVTPLT LGIETLGGVA TPLIPRNTTI PVTKSQVFST AADNQSEVTI SVVQGERPMA
     SDNKQLGQFN LSGIEPAPRG VPQIEVSFSI DVNGITTVKA KDLKTNKEQE ITIKNSSKLS
     DEEVEKMVKE AEENREADKA KKEKVEVIVR AESLISQLEK SLVDQGDKVD AKAKEETQKQ
     IQELKDLIKD DKIEELKVKL EQIEQAAQAF AQYSAQQAAT ENSKDSDTVE AEIVDDKAN