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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
 
 
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