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EFG_NEIMB
ID   EFG_NEIMB               Reviewed;         701 AA.
AC   Q9K1I8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=NMB0138;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17038831; DOI=10.4161/hv.1.2.1651;
RA   Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.;
RT   "Characterization of the protein content of a meningococcal outer membrane
RT   vesicle vaccine by polyacrylamide gel electrophoresis and mass
RT   spectrometry.";
RL   Hum. Vaccin. 1:80-84(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=NZ98/254 / Serogroup B;
RX   PubMed=16645985; DOI=10.1002/pmic.200500821;
RA   Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT   "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT   prepared from the group B strain NZ98/254.";
RL   Proteomics 6:3400-3413(2006).
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome changes
CC       from the pre-translocational (PRE) to the post-translocational (POST)
CC       state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC       deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC       coordinated movement of the two tRNA molecules, the mRNA and
CC       conformational changes in the ribosome. {ECO:0000255|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
CC   -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC       used as vaccines in human.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00054}.
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DR   EMBL; AE002098; AAF40597.1; -; Genomic_DNA.
DR   PIR; C81234; C81234.
DR   RefSeq; NP_273196.1; NC_003112.2.
DR   RefSeq; WP_002218568.1; NC_003112.2.
DR   AlphaFoldDB; Q9K1I8; -.
DR   SMR; Q9K1I8; -.
DR   STRING; 122586.NMB0138; -.
DR   PaxDb; Q9K1I8; -.
DR   EnsemblBacteria; AAF40597; AAF40597; NMB0138.
DR   KEGG; nme:NMB0138; -.
DR   PATRIC; fig|122586.8.peg.178; -.
DR   HOGENOM; CLU_002794_4_1_4; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00484; EF-G; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..701
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091168"
FT   DOMAIN          8..290
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   701 AA;  77244 MW;  27FF7781B4A40B0D CRC64;
     MARKTPISLY RNIGISAHID AGKTTTTERI LFYTGLTHKL GEVHDGAATT DYMEQEQERG
     ITITSAAVTS YWSGMAKQFP EHRFNIIDTP GHVDFTVEVE RSMRVLDGAV MVYCAVGGVQ
     PQSETVWRQA NKYQVPRLAF VNKMDRQGAN FFRVVEQMKT RLRANPVPIV IPVGAEDNFS
     GVVDLLKMKS IIWNEVDKGT TFTYGDIPAE LVETAEEWRQ NMIEAAAEAS EELMDKYLGG
     DELTEEEIVG ALRQRTLAGE IQPMLCGSAF KNKGVQRMLD AVVELLPAPT DIPPVQGVNP
     NTEEADSRQA SDEEKFSALA FKMLNDKYVG QLTFIRVYSG VVKSGDTVLN SVKGTRERIG
     RLVQMTAADR TEIEEVRAGD IAAAIGLKDV TTGETLCAES APIILERMEF PEPVIHIAVE
     PKTKADQEKM GIALNRLAKE DPSFRVRTDE ESGQTIISGM GELHLEIIVD RMKREFGVEA
     NIGAPQVAYR ETIRKAVKAE YKHAKQSGGK GQYGHVVIEM EPMEPGGEGY EFIDEIKGGV
     IPREFIPSVD KGIRDTLPNG IVAGYPVVDV RIRLVFGSYH DVDSSQLAFE LAASQAFKEG
     MRQASPALLE PIMAVEVETP EEYMGDVMGD LNRRRGVVLG MDDDGIGGKK VRAEVPLAEM
     FGYSTDLRSA TQGRATYSME FKKYSEAPAH IAAAVTEARK G
 
 
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