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HTPG_MARN8
ID   HTPG_MARN8              Reviewed;         630 AA.
AC   A1TZH7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=Maqu_1054;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM18146.1; -; Genomic_DNA.
DR   RefSeq; WP_011784564.1; NC_008740.1.
DR   AlphaFoldDB; A1TZH7; -.
DR   SMR; A1TZH7; -.
DR   STRING; 351348.Maqu_1054; -.
DR   PRIDE; A1TZH7; -.
DR   EnsemblBacteria; ABM18146; ABM18146; Maqu_1054.
DR   KEGG; maq:Maqu_1054; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000998; 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; 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; Stress response.
FT   CHAIN           1..630
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014928"
FT   REGION          1..338
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          339..555
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          556..630
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   630 AA;  71534 MW;  0A73257B469E7FE8 CRC64;
     MTVEANKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAEDKLR FAALKDDKLF
     EGDSDLKIRL DYDKDAGTIT IADNGIGMTR DDVIANLGTI AKSGTAEFLK QLSGDEKKDS
     KLIGQFGVGF YSAFIVADKV EVFTRKAGEP ADNGVHWESK GDGEFTIEPV SREQRGTEIV
     LHLKPEDKEF ADGWKLRSLV KKYSDHISFP VVMKSESEEE DKKGEEETVN DATALWTLPR
     TEIKDEEYKE FYKHIAHDFE DPLTWSHNKV EGKLDYTSLL YIPKRAPFDL YNREAPRGLK
     LYVQRVFIMD DAEQFLPLYL RFTKGVIDSN DLSLNVSREI LQNDSTVESI RTALTKRVLD
     MLSKLAKKGG DEYQGFWDEF GTVLKEGPAE DFSNREKIAG LLRFASTHTG EATQNVSLDD
     YISRMKEGQN KIYYITGDNF AAAKSSPHLE VFRKKGIEVL ILSDRIDEWM MGYLSEYDGK
     QFQDVARGDL DLGEVETEED KKHQEEAAKE HKDLLERIKT ALEDQVQEVR VTNRLTDSPA
     CLVVGQFDMG AQMKKIMEAA GQKVPESKPI FEINVDHPLV QRLETEQGEQ RFKELSAVLF
     DQATLASGEQ LKDPGAYVSR LNRLLLELAN
 
 
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