(data stored in ACNUC30630 zone)

SWISSPROT: EFG_BIFAA

ID   EFG_BIFAA               Reviewed;         709 AA.
AC   A1A0T0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   11-DEC-2019, entry version 86.
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=BAD_0532;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; AP009256; BAF39313.1; -; Genomic_DNA.
DR   RefSeq; WP_003808605.1; NC_008618.1.
DR   SMR; A1A0T0; -.
DR   PRIDE; A1A0T0; -.
DR   EnsemblBacteria; BAF39313; BAF39313; BAD_0532.
DR   GeneID; 4557240; -.
DR   KEGG; bad:BAD_0532; -.
DR   eggNOG; ENOG4105CEJ; Bacteria.
DR   eggNOG; COG0480; LUCA.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; AATTCHW; -.
DR   BioCyc; BADO367928:G1G2R-578-MONOMER; -.
DR   Proteomes; UP000008702; Chromosome.
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; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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   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; TF_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_II; 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;
DR   PRODOM; A1A0T0.
DR   SWISS-2DPAGE; A1A0T0.
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..709
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000008804"
FT   DOMAIN          10..295
FT                   /note="tr-type G"
FT   NP_BIND         19..26
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   NP_BIND         91..95
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   NP_BIND         145..148
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   709 AA;  78466 MW;  72ECFC75070BFC85 CRC64;
     MALDVLNDLN QIRNIGIMAH IDAGKTTTTE RILFYTGKNY KIGETHDGAS TMDFMAQEQE
     RGITIQSAAT TCFWNRQTHD EKQKFQINII DTPGHVDFTA EVERSLRVLD GAVAVFDGKE
     GVEPQSETVW RQADKYGVPR ICFINKMDKL GADFYYSVDT IKTKLGATPL VVQLPIGAEN
     DFAGVVDLIR MKAYVWNDVS GDLGAHYDTT DIPADLQDKA EQYRSELLDQ VAESDEELLE
     KYLESGELTE DEIRAGIRKL TINREAYPVL CGSAFKDKGV QPMLDAVVDY LPSPEDVPSI
     VGFDPQDESI EIDRKPTTDD PFSALVFKIS THPFYGKLVF VRVYSGSVKP GDTVLDSTKE
     KKERVGKIFQ MHADKENPVD AAEAGNIYTF VGLKNVTTGD TLCDEKSPIS LESMTFPDPV
     IEVAVEPKTK ADQEKMSIAL AKLSDEDPTF QVKTDEESGQ TLISGMGELQ LDIIVDRMRR
     EFKVECNVGN PQVAYRETIR KAVMNQEYTH KKQTGGSGQF AKVLMNFEPL DTENGETYEF
     VNEVTGGHIT KEFIPSIDAG VQEAMESGIL AGFPVVGVKA TVTDGQVHDV DSSEMAFKIA
     GSMCFKEAAP KAKPVILEPI MAVEVRTPEE YMGDVMGDIN ARRGSIQSMT DSTGVKVIDA
     KVPLSEMFGY IGDLRSKTQG RAMFTMQMDS YAEVPKNVSE EIIKAQRGE
//

If you have problems or comments...

PBIL Back to PBIL home page