DNAK_MESH2
ID DNAK_MESH2 Reviewed; 600 AA.
AC Q49539; Q601X9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=65 kDa protein;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
DE AltName: Full=P65;
GN Name=dnaK; OrderedLocusNames=mhp072;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chou S.Y., Shiuan D.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV27395.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U50209; AAB01921.1; -; Genomic_DNA.
DR EMBL; AE017332; AAV27395.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044284771.1; NC_006360.1.
DR AlphaFoldDB; Q49539; -.
DR SMR; Q49539; -.
DR STRING; 295358.mhp072; -.
DR EnsemblBacteria; AAV27395; AAV27395; mhp072.
DR KEGG; mhy:mhp072; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_14; -.
DR PhylomeDB; Q49539; -.
DR Proteomes; UP000006822; 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; 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..600
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078492"
FT REGION 570..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 600 AA; 65575 MW; 1F928F72EABBDB6B CRC64;
MAKEIILGID LGTTNSVVAI IENQKPVVLE NPNGKRTTPS VVAFKNNEEI VGDAAKRQLE
TNPEAIASIK RLMGTDKTVR ANERDYKPEE ISAKILAYLK EYAEKKIGHK VTKAVITVPA
YFDNAQREAT KNAGKIAGLQ VERIINEPTA AALAFGLDKT EKEMKVLVYD LGGGTFDVSV
LELSGGTFEV LSTSGDNHLG GDDWDNEIVN WLVKKIKEVY DFDPKSDKMA LTRLKEEAEK
TKINLSNQSV STVSLPFLGM GKNGPINVEL ELKRSEFEKM TAHLIDRTRK PIVDALKQAK
IEASDLDEVL LVGGSTRMPA VQSMIEHTLN KKPNRSINPD EVVAIGAAIQ GGVLAGEISD
VLLLDVTPLT LGIETLGGIA TPLIPRNTTI PVTKSQIFST AEDNQTEVTI SVVQGERQLA
ADNKMLGRFN LSGIEAAPRG LPQIEVSFSI DVNGITTVSA KDKKTGKEQT ITIKNTSTLS
EEEINKMIQE AEENREADAL KKDKIETTVR AEGLINQLEK SITDQGEKID PKQKELLEKQ
IQELKDLLKE DKTDELKLKL DQIEAAAQSF AQATAQQANT SESDPKADDS NTIDAEIKQD