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EFG1_BORA1
ID   EFG1_BORA1              Reviewed;         700 AA.
AC   Q2L2H1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Elongation factor G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA1 {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=BAV0022;
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}.
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DR   EMBL; AM167904; CAJ47606.1; -; Genomic_DNA.
DR   RefSeq; WP_012415732.1; NC_010645.1.
DR   AlphaFoldDB; Q2L2H1; -.
DR   SMR; Q2L2H1; -.
DR   STRING; 360910.BAV0022; -.
DR   PRIDE; Q2L2H1; -.
DR   EnsemblBacteria; CAJ47606; CAJ47606; BAV0022.
DR   GeneID; 41391951; -.
DR   KEGG; bav:BAV0022; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_4; -.
DR   OMA; MDDMVGG; -.
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..700
FT                   /note="Elongation factor G 1"
FT                   /id="PRO_0000263428"
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   700 AA;  77128 MW;  ADAA6F1CFFBA767A CRC64;
     MARKTPIERY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG
     ITITSAATTA FWRGMAGNFP EHRINIIDTP GHVDFTIEVE RSMRVLDGAC MVYCAVGGVQ
     PQSETVWRQA NKYGVPRLAF VNKMDRTGAN FFKVYEQLRT RLRANPVPIV IPIGAEDTFT
     GVIDLVKMKA IIWDEASQGT KFEYADIPAE LQASAEEWRE KLVEAAAESS EELMNKYLET
     GTLEEAEINA AIRQRTIAGE IHPMLCGTAF KNKGVQRMLD AVIEYLPSPI DIPPVDGTDD
     DGNEVQRRAD DSEKFSALAF KLMSDPFVGQ LTFVRVYSGV LKSGDTVYNP IKGKKERIGR
     ILQMHANNRE EIKEVLAGDI AAVVGLKDVT TGETLCDIDA HVTLERMEFP EPVISQAVEP
     KSKADQEKMG LALSRLAQED PSFRVRSDEE SGQTIISGMG ELHLEILVDR MKREFGVEAN
     VGKPQVAYRE TIRKTCDEVE GKFVKQSGGR GQYGHVVLKV EPLAPGGGYE FVDAIKGGVV
     PREYIPAVDK GIQETLPAGI LAGYPVVDVK VTLFFGSYHD VDSNENAFKM AGSMAFKEGM
     RKASPVLLEP MMAVEVETPE DYAGGVMGDL SSRRGMVQGM DDMVGGGKII KAEVPLAEMF
     GYATNLRSLT QGRATYTMEF KHYSEAPKNV ADEVIAARGK
 
 
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