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EFG_LEPIN
ID   EFG_LEPIN               Reviewed;         706 AA.
AC   Q8F983;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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}; Synonyms=fusA1;
GN   OrderedLocusNames=LA_0313;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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   -!- 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; AE010300; AAN47512.1; -; Genomic_DNA.
DR   RefSeq; NP_710494.1; NC_004342.2.
DR   RefSeq; WP_000102023.1; NC_004342.2.
DR   AlphaFoldDB; Q8F983; -.
DR   SMR; Q8F983; -.
DR   STRING; 189518.LA_0313; -.
DR   EnsemblBacteria; AAN47512; AAN47512; LA_0313.
DR   GeneID; 61143624; -.
DR   KEGG; lil:LA_0313; -.
DR   PATRIC; fig|189518.3.peg.315; -.
DR   HOGENOM; CLU_002794_4_1_12; -.
DR   InParanoid; Q8F983; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 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; IPR045044; EFG1-like.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/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   PANTHER; PTHR43636; PTHR43636; 1.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..706
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091145"
FT   DOMAIN          15..291
FT                   /note="tr-type G"
FT   BINDING         24..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         145..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   706 AA;  79001 MW;  BDF1062A1028E33F CRC64;
     MSTAVAEFKP SEKLLKTRNI GISAHIDSGK TTLTERILFY TNRIHAIHEV RGKDGVGAKM
     DSMDLERERG ITIQSAATYC QWKNHTINII DTPGHVDFTV EVERSLRVLD SAILVLCGVA
     GVQSQSITVD RQMRRYNVPR VAFINKLDRT GANPFRVIEQ LKEKLKHNAV PVQIPIGLEN
     DLKGIVDLVT MKAYYFEGKD GMDIQEKEIP DDLKELAQKK HEELLDAASM FSDELTEALL
     EGTPTEEMIK KAIRTGTIEL KMTPVFMGSA FKNKGVQKLL DGVLDYLASP VDVKNKALDQ
     NNNEEMIVLE SNFEKPLVCL AFKLEDGRYG QLTYVRVYQG KLAKGMTIYN MSNNKKHNVG
     RLCRMHSDEM EDIDSAEAGD IIALFGIDCA SGDTFTDGKL KVSMESMFVP APVISLTIEA
     KESKHLNNLA KALNRFTKED PTFQTHVDQE SGQTIIKGMG ELHLEVYIER MKREYGVELI
     TGAPQVAYRE TITSKADFDY THKKQTGGQG QFGRVAGYME PIPLEETLDY DFVNKVVGGA
     IPREYIQSVD KGFKSCLERG SLIGFPIIGV RCVINDGAYH DVDSSDMAFQ IAGRYAFRQG
     FNKANPQILE PIMKVEVDGP SEFQGAILGS LNQRRGMILN TTEEDAYCKT EAEVPLADMF
     GYSTVLRSST QGKAEFSMEF SRYAPVPRNV AEELMKKYKV NNKDED
 
 
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