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HTPG_PELPD
ID   HTPG_PELPD              Reviewed;         645 AA.
AC   A1ANS1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Ppro_1375;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) 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; CP000482; ABK98991.1; -; Genomic_DNA.
DR   RefSeq; WP_011735284.1; NC_008609.1.
DR   AlphaFoldDB; A1ANS1; -.
DR   SMR; A1ANS1; -.
DR   STRING; 338966.Ppro_1375; -.
DR   PRIDE; A1ANS1; -.
DR   EnsemblBacteria; ABK98991; ABK98991; Ppro_1375.
DR   KEGG; ppd:Ppro_1375; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000006732; 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   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..645
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014937"
FT   REGION          1..348
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          349..565
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          566..645
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   645 AA;  73943 MW;  2CB0F667BDA78411 CRC64;
     MSKTTKQFQT EVKQLLDLVI HSLYSNRDIF LRELISNSSD AIDKIRFEAH SNEELLEGNS
     DWKIKLIPDK DAGTLTILDN GIGMTMAEVE ENIGTIARSG TKAFMQALKD KSATDNPELI
     GQFGVGFYAS FMVADRVILE TRKGGTASDG CRWESIGDGS YTIEECSLDR RGTEIVLHLK
     DEFKEYLEEW KIRSIVKKYS DYIQYPVVMD ITRTETPKGV DGEEIEGAGT IEKTVEETLN
     SMKAIWARPK SEVTEEEYQE FYKHISHDFE NPFNTIHFSA EGISEFKALI YLPAKKPFDL
     FMADRKKGLQ LYVKRVFITD RCEELLPDYL RFVKGVVDSS DLPLNVSREI LQEDVQIKRI
     QKSLVGKILS TLAEVKEKNF DEYVNFWKEF GPVLKEGLHF DYANKEKLQE LALFESTATE
     AGSFTSLKEY VERMPEAQQE IYFITGDSRA TLKISPHLEA FKAKGYEVLF LTDPVDEWVV
     QALTEYKEKK LKAVDRGDVD LDSEEEKKEK ETKQEEARKE YGDLISFIKS HLEDRVKDAR
     LSKRLTDSAC CLVADEYGIN ANMERILKAM NQPVPDSKRV LELNPDHPIM KIMTEIFREN
     KEDARLTDYA DLLYDQALLT EGSPIKDPLR FTRLVSELMV KAATK
 
 
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