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HTPG_WOLPM
ID   HTPG_WOLPM              Reviewed;         635 AA.
AC   P61189;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=WD_1277;
OS   Wolbachia pipientis wMel.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=163164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA   Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA   McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA   Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA   Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA   Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA   O'Neill S.L., Eisen J.A.;
RT   "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT   streamlined genome overrun by mobile genetic elements.";
RL   PLoS Biol. 2:327-341(2004).
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; AE017196; AAS14921.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61189; -.
DR   SMR; P61189; -.
DR   STRING; 163164.WD_1277; -.
DR   EnsemblBacteria; AAS14921; AAS14921; WD_1277.
DR   KEGG; wol:WD_1277; -.
DR   eggNOG; COG0326; Bacteria.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000008215; 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; 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; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
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; Stress response.
FT   CHAIN           1..635
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063025"
FT   REGION          1..337
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          338..556
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          557..635
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   635 AA;  72668 MW;  C88BA6F0CC773F5E CRC64;
     MELKMHNVQE TENLKFDAEV GKVLNIVIHS LYTNKDIFLR ELISNASDAC DKLRYESQLN
     PNLLDLSDEL KITISSNKDK NELYITDNGI GMNRQDLIDN LGTIASSGTQ KFLDAIKNSK
     DSSQTVELIG KFGVGFYSSF MVASEVIVES RKAGEEESWI WQSKGDGEYS ISKSDNQVPR
     GTKITLIMHP EENEFLDKFR VENIVTTYSD HINFPVEFID EEGKSEKLNS KAAIWTKPKN
     DVTQEEHNDF FRSVAHVGGE PWMILHNKNE GAIEYTNLLY VPSIKPFDLF HPDRRCSVKL
     YVNKVFITED NVQIIPQYLR FLKGIVDSPD LPLNISRETL QNNRVVEQIR KSLTKRAISE
     LGKKAKENLE EYTKFWTNFG AVLKEGLCEA MPTDEREALL SICRFHSTGD EKLVSIDDYI
     SRMKPEQEHI YYLTGNSLDS VKNSPQLEGF VSKGLEVLLF VDPVDDFWTS VIHEYKDQKI
     KSVTRADVDL EKFSSEEDKT DEENKSNEEK TEETILQYFT TVLGDSVKSV KISKKLTDSP
     VCLAVDEGAM DLRMERFLRE QKQLNYRTPK VLEINTKHPL IKSIMKSYAE SGENPTLEDM
     IHLLFYQACI VEGEEMDDVS LFAKRLNNLL GKISV
 
 
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