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HTPG_METS4
ID   HTPG_METS4              Reviewed;         611 AA.
AC   B0UN89;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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}; OrderedLocusNames=M446_0044;
OS   Methylobacterium sp. (strain 4-46).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4-46;
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., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL   Submitted (FEB-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; CP000943; ACA14632.1; -; Genomic_DNA.
DR   RefSeq; WP_012330050.1; NC_010511.1.
DR   AlphaFoldDB; B0UN89; -.
DR   SMR; B0UN89; -.
DR   STRING; 426117.M446_0044; -.
DR   EnsemblBacteria; ACA14632; ACA14632; M446_0044.
DR   KEGG; met:M446_0044; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
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; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..611
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127032"
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..611
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   611 AA;  67209 MW;  1D5B0B5A06155AFA CRC64;
     MSETLERHAF GAEVGRLLDL VVHALYSERE IFLRELVANA ADAVDRRRFG ALTDPALSLP
     ADAKVRIRPD KAARTLAISD PGIGMSKEDL AQNLGTIARS GTRAFSQSLA DAKPDERPSL
     IGQFGVGFYS AFMVADRVEV TSRKAGSDEA WTWASEGQGE YTLSPATRAE PGTDVVLHIK
     ADADEYLEPL RLETIVRKWA DHITVPITLL RDGEEVSGNE GTALWRKPKS EVSEEAYTAF
     YRHVTHNFDA PWATLHWRAE GALDFTALLF IPGMKPFLAV EEERESRVRL HVRRMFITDE
     AGLLPSWLRF VQGVVDTEDL PLNVSREMLQ ATPVLARIRR AVTGKVMAEL KSRAKDAESY
     ATFWQAFGPV LKEGIWEDAE HRDDIAALLR FRSTAVEGWT SFADYVSRMK PNQEAIYILV
     GDDAAALARS AQIEGFRARG IEVLLLSDHV DAFWPERLDK FDGKPIRSIT QSADDLSAFA
     PEGEAAGEAA DLTELLPKLK EILKDDVAEV RASQRLVESA VLLSASSGGP DLQMQRLLRR
     AGRGFGAGLP VLELNPRHAL VRRIAERARA GEDVGEAAQT LLDLAHVQGG DPPRDPVAFA
     RRVAAALAAQ A
 
 
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