GenomeNet

Database: UniProt
Entry: B2IK59
LinkDB: B2IK59
Original site: B2IK59 
ID   EFG_BEII9               Reviewed;         691 AA.
AC   B2IK59;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   29-OCT-2014, entry version 45.
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};
GN   OrderedLocusNames=Bind_1351;
OS   Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB
OS   8712).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Beijerinckiaceae; Beijerinckia.
OX   NCBI_TaxID=395963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9039 / DSM 1715 / NCIB 8712;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Dunfield P.F., Dedysh S.N., Liesack W., Saw J.H., Alam M., Chen Y.,
RA   Murrell J.C., Richardson P.;
RT   "Complete sequence of chromosome of Beijerinckia indica subsp. indica
RT   ATCC 9039.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome
CC       changes from the pre-translocational (PRE) to the post-
CC       translocational (POST) state as the newly formed A-site-bound
CC       peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC       sites, respectively. Catalyzes the coordinated movement of the two
CC       tRNA molecules, the mRNA and conformational changes in the
CC       ribosome. {ECO:0000255|HAMAP-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}.
CC   -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding)
CC       domain. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001016; ACB94991.1; -; Genomic_DNA.
DR   RefSeq; YP_001832480.1; NC_010581.1.
DR   ProteinModelPortal; B2IK59; -.
DR   STRING; 395963.Bind_1351; -.
DR   PRIDE; B2IK59; -.
DR   EnsemblBacteria; ACB94991; ACB94991; Bind_1351.
DR   GeneID; 6199245; -.
DR   KEGG; bid:Bind_1351; -.
DR   PATRIC; 21085513; VBIBeiInd21058_1697.
DR   eggNOG; COG0480; -.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; KQYAETP; -.
DR   OrthoDB; EOG6X6RBF; -.
DR   BioCyc; BIND395963:GJA7-1371-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR000795; EF_GTP-bd_dom.
DR   InterPro; IPR009022; EFG_III-V.
DR   InterPro; IPR000640; EFG_V.
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; IPR009000; Transl_B-barrel.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
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; 2.
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   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    691       Elongation factor G.
FT                                /FTId=PRO_1000091692.
FT   DOMAIN        8    283       tr-type G.
FT   NP_BIND      17     24       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
FT   NP_BIND      81     85       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
FT   NP_BIND     135    138       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
SQ   SEQUENCE   691 AA;  76325 MW;  96755F1B358F5EAC CRC64;
     MPRSHPIEDY RNFGIMAHID AGKTTTTERI LYYSGKSHKI GEVHDGAATM DWMEQEQERG
     ITITSAATTT FWNGRRLNII DTPGHVDFTI EVERSLRVLD GAVCVLDGNQ GVEPQTETVW
     RQADKYNVPR IVFVNKMDKI GADFYRCVED IKTKVGGRPV CIQLPIGSEA DFKGIIDLVR
     MKAVVWEDEA LGAKYHDEEI PDDLKEKAIH YRNLLVEAAV ELDDDAMTAY LEGVEPDEAL
     LKLLIRKAVR QITFIPVLCG SAFKNKGVQP LLDAVVDYLP TPIDREAIKG VDVNTGEETV
     RLPSDSEPFS MLAFKIMDDP FVGSITFARV YSGKIESGTS VVNSTKDKKE RIGRMLLMHA
     NNREDIKEAY AGDIVALAGL KETRTGDTLC DVNKPVILER MEFPEPVIEI AIEPKSKADQ
     EKLGIALSKL AAEDPSFRVS TDQESGQTIL KGMGELHLDI KVDILKRTYK VDANIGAPQV
     AYREKLMRRV EIDETHKKQT GGTGQFARVK MIFEPNEAAA GNAFESNIVG GAVPKEYIPG
     VEKGLYSVLN SGVLAGFPVV DVKATLIDGA FHEVDSSVLA FEICSRAATR RALKEGGSVL
     LEPIMKVEVT TPEEYTGSVM GDLLGRRGQV QGQDMRGNAV VINAMVPLAN MFGYVNQLRS
     FSQGRANYSM QFDHYEQVPA NEAAKVQAKY A
//
DBGET integrated database retrieval system