ID   DNAK_METHO              Reviewed;         595 AA.
AC   Q9ZEJ0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Metamycoplasma hominis (Mycoplasma hominis).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC   Metamycoplasma.
OX   NCBI_TaxID=2098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FBG;
RA   Henrich B., Bernhardt A.;
RT   "DnaK-like protein of Mycoplasma hominis.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AJ132792; CAA10785.1; -; Genomic_DNA.
DR   RefSeq; WP_020002506.1; NZ_QOKO01000016.1.
DR   AlphaFoldDB; Q9ZEJ0; -.
DR   SMR; Q9ZEJ0; -.
DR   PATRIC; fig|2098.16.peg.539; -.
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   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..595
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078491"
FT   REGION          573..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         176
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   595 AA;  65623 MW;  2609F0E554DAC3E1 CRC64;
     MAKEFILGID LGTTNSVVSV IENGTPKILE NPNGKRTTPS VVAFKNGETI IGESAKRQLE
     SNKDSVASIK RLMGTSQTVH LNNKDYKPEE ISAMILSYMK DYADKKLGQP VKKAVITVPA
     YFDNAQREAT KNAGIIAGLD VVRIINEPTA AALAFGLNKD KNENQKILVF DLGGGTFDVS
     LLEMESGTFE VLATAGDNHL GGDDWDHEIV KWMVEQIKSK YNFDPTTDKM AMARLKEEAE
     RAKITLSEQL IANISLPFLA MNENGPVNVE LEITRATFES MTEHLLQRTR KPLLDVLSEA
     KLTWNDINEV LLVGGSTRMP AVQKLVAEVT NKKPNNSINP DEVVSVGAAI QGAILAGEIQ
     DVLLLDVTPL TLGIVVEGDV VAPLIPRNTT IPVTKSQIFS TAVDNQTAVT IVITQGERQL
     ARDNKILGQF NLEGIEPAPR GIPQIEVSFS IDVNGITKVT AKDKKTNKEQ TITIQNTSSL
     SKEEVEKMVK DAEANREADQ KKRHEIEVIV KAEQLSNDLE KTLKSEQAKN LGEPQKQELQ
     KEIDEIKELI NKKDIEQLEK KITEFEQKMA QAAEFLKKQQ GNNNPNTNND NPQTN