EFG_XANOR
ID EFG_XANOR Reviewed; 705 AA.
AC Q5GWS9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=XOO3588;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAW76842.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE013598; AAW76842.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011260031.1; NC_006834.1.
DR AlphaFoldDB; Q5GWS9; -.
DR SMR; Q5GWS9; -.
DR STRING; 291331.XOO3588; -.
DR EnsemblBacteria; AAW76842; AAW76842; XOO3588.
DR KEGG; xoo:XOO3588; -.
DR HOGENOM; CLU_002794_4_1_6; -.
DR Proteomes; UP000006735; 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"
FT /id="PRO_0000225252"
FT DOMAIN 8..290
FT /note="tr-type G"
FT REGION 290..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 77608 MW; 46AC0F008A5B7BA4 CRC64;
MARTTPIERY RNFGIMAHID AGKTTTSERI LFYTGVSHKI GEVHDGAAVM DWMEQEQERG
ITITSAATTA FWSGMDKSMP QHRFNIIDTP GHVDFTIEVE RSLRVLDGAV FVLCAVGGVQ
PQSETVWRQA NKYSVPRMAF VNKMDRTGAN FDKVVEQLKA RLGAYAVPMQ VPIGAEDGFE
GVVDLLKMKA IHWDTASQGT TFEYSDIPAE LVDVATDARS FMVEAAAEAS EDLMDKYLNE
GDLSEEEILK GLRERTLKVE IVPVFCGSAF KNKGVQAMLD GVVHLLPSPA DRPPVQGIDE
DEKEDTRAAT DTAPFSALAF KIMTDPFVGS LTFFRVYSGT LNSGDQVYNP VKSKKERVGR
ILQMHSNNRE EIKEVRAGDI AAAVGLKDVT TGDTLCAQDK IITLERMVFP EPVISMAVEP
KTKSDQEKMG MALGRLAQED PSFRVKTDEE SGQTIISGMG ELHLDIIVDR MRREFNVEAN
VGKPQVAYRE TIRKSDVKSD YKHAKQSGGK GQYGHVVIEL SPMTEEDRKS DNVKDDFLFI
NDITGGIIPK EFIPSVEKGL RETITSGPIA GFPVVGVKVK LVFGSYHDVD SSEMAFKLAA
SMAFKQGFAK ASPVLLEPIM KVEIVSPEDY LGDVMGDVSR RRGVLQGQDD SPSGKIINAM
IPLGEMFGYA TSLRSMSQGR ATFSMEFDHY EEAPANIADA VTKKG
