EFG2_BORA1
ID EFG2_BORA1 Reviewed; 705 AA.
AC Q2KV83;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Elongation factor G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA2 {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=BAV2919;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM167904; CAJ50529.1; -; Genomic_DNA.
DR RefSeq; WP_012418558.1; NC_010645.1.
DR AlphaFoldDB; Q2KV83; -.
DR SMR; Q2KV83; -.
DR STRING; 360910.BAV2919; -.
DR PRIDE; Q2KV83; -.
DR EnsemblBacteria; CAJ50529; CAJ50529; BAV2919.
DR GeneID; 41394759; -.
DR KEGG; bav:BAV2919; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_4; -.
DR OMA; NHKMGEV; -.
DR OrthoDB; 88967at2; -.
DR Proteomes; UP000001977; 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 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..705
FT /note="Elongation factor G 2"
FT /id="PRO_0000263429"
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 705 AA; 78035 MW; 24A06BAE0975F7F0 CRC64;
MTRRTPIELY RNIGISAHID AGKTTTTERI LFYTGITHKL GEVHEGAAVM DWMEQEQERG
ITITSAATTA FWRGMAGNYP EHRINIIDTP GHVDFTIEVE RSMRVLDGAC MVYDSVGGVQ
PQSETVWRQA NKYRVPRIAF VNKMDRIGAD FLRVQRQIVE RLKGDAVPVQ LPIGAEDNFQ
GVVDLVKMKA ILWDEASQGV SFKYEDVPAP MLELANQWRD KLVEKAAEAN EVLLEKYLSG
EALSEEEIKT GLRQRTIANE IVPMLCGSAF KNKGVQAMLD AVLDYLPSPL DVPAIKGHDE
HDKEIERRPS DKDPFSALAF KIMTDPFVGQ LVFFRAYSGV VKSGDSVLNP LKNKKERLGR
ILQMHANERK EINEVYAGDI AAAVGLKDVT TGDTLTDPGH VIILERMIFP EPVISQAVEP
KTKADQEKMS LALNRLAQED PSFRVRTDEE SGQTIISGMG ELHLEILVDR MKREFNVEAT
VGKPQVAYRE TIRKKVEGVE GKFVKQSGGR GQYGHAVITV EPQAAGKGFE FIDAIKGGVI
PREFIPAVER GIVDTLNTGV LAGYPVVDVK VTLTFGSYHD VDSNENAFRM AGSMAFKEGL
RRATPVLLEP MMQVEVETPE DFTGNVMGDL SSRRGMVQGM EDIAGGGGKL VRAEVPLAEM
FGYSTSLRSL TQGRATYSME FKHYAEAPRQ VAEQVIAART GSTRA
