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HTPG_METRJ
ID   HTPG_METRJ              Reviewed;         610 AA.
AC   B1LZG0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505};
GN   OrderedLocusNames=Mrad2831_5467;
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR   EMBL; CP001001; ACB27412.1; -; Genomic_DNA.
DR   RefSeq; WP_012322355.1; NC_010505.1.
DR   AlphaFoldDB; B1LZG0; -.
DR   SMR; B1LZG0; -.
DR   STRING; 426355.Mrad2831_5467; -.
DR   EnsemblBacteria; ACB27412; ACB27412; Mrad2831_5467.
DR   KEGG; mrd:Mrad2831_5467; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000006589; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..610
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127031"
FT   REGION          1..326
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          327..536
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          537..610
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   610 AA;  67040 MW;  88FEFC5AFE49A647 CRC64;
     MSETIERHEF GAEVGRLLDL VVHALYSDRE IFLRELVANA ADAMDRRRFE ALTSAASALP
     PDAKVRIAPD KEARTLTVSD AGIGMTKEDL ATNLGTIARS GTRAFSQTLE SAKAEDRPSL
     IGQFGVGFYS AFMVADRVTV TSRRAGSDEA WTWASEGQGS YTLEPATRAE PGTDIVLHLK
     ADADEYLEPY RLDHLVRKWA DFITVPIAVV RDGKDESANQ GTALWRKAKS EVTEEQYEEF
     YHSIGMNFDK PWATLHWRAE GQLEFSALLF IPGSKPFQAL ENERQSKVRL HVRRMFITDE
     AELLPPWLRF VQGVVDTEDL PLNVSREMLQ STPALARIRR AVTGRVVSEL TTRAKDAEGY
     QSFWENFGPV LKEGIYEDFE RRGEIAPLLR FRSSAVEGWT SLPDYVSRMK DGQEAIYYLV
     ADDAEALKSS PQLEGFRARG LEVLLLSDHV DAFWPDQLGT FDGKPLRSIT KGGLDLSKFA
     LEGEQPEAPE GIDAFVAAVK TALGAEVSDV RTTDRLVDSA VVLSAGSGGP DLQMQRLMRR
     AGRAGAGQPV LEINPRHPLI RALAAAPESE VPQAAGTLLD LARIQDGDSP RDPAAFARTV
     AAALAAARGA
 
 
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