EFG_PHYAS
ID EFG_PHYAS Reviewed; 688 AA.
AC B1VAM2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=PA0661;
OS Phytoplasma australiense.
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX NCBI_TaxID=59748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18359806; DOI=10.1128/jb.01301-07;
RA Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT and AY-WB.";
RL J. Bacteriol. 190:3979-3991(2008).
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; AM422018; CAM11995.1; -; Genomic_DNA.
DR RefSeq; WP_012359123.1; NC_010544.1.
DR AlphaFoldDB; B1VAM2; -.
DR SMR; B1VAM2; -.
DR STRING; 59748.PA0661; -.
DR EnsemblBacteria; CAM11995; CAM11995; PA0661.
DR KEGG; pal:PA0661; -.
DR eggNOG; COG0480; Bacteria.
DR OMA; AATTCHW; -.
DR Proteomes; UP000008323; 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..688
FT /note="Elongation factor G"
FT /id="PRO_1000201480"
FT DOMAIN 8..282
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 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 688 AA; 76234 MW; 1B3987FBF4AD1D47 CRC64;
MARQFTLEKT RNIGIIAHID AGKTTTTERI LFHTGKIHKI GETHDGASQM DWMEQEQERG
ITITSAATTA FWKDHRVNII DTPGHVDFTV EVSRSLRVLD GAVTVIDAQA GVEPQTETVW
RQATEYKAPR IIFVNKMDKI GANFEYAVET LNQRLGVHAN PIQWPIGAEN DFTGIIDLVT
LTAFEYDGSP EEKGKPIPIP SSLQDVAELK RNELIESLSN LDEELMLLYL EEKPISAEVL
KKAIRKATLQ ASFFPVLCGS SFKNKGVVKM LDAIVDYLPA PCDVAPIVGI DEKNKEITRL
NSDEEPFTAL AFKVMTDPYV GKLTFFRIYA GKVNSGSYVF NTTKGTKERF GRLLQMHANS
REEVKEAYAG DILAVVGLKG TTTGDTLAAE GQTIVLESMN FPEPVIEIAV EPKTKADQDK
MGIALSKLAE EDPTFRVFSN HETGQTIIAG MGELHLDIIM ERLKREFKIQ ANTTAPQVAY
RETITQETET EGKFIRQSGG RGQYGHVWMR FEPNPGKGFE FVNKIVGGVV PREYVPAVQK
GIQEALAGGI LAGYPIVDIK ATLFDGSYHD VDSSEMAFKI AASMSLKETK TKGNPVILEP
IMNVEVVTPN DYVGNVIGDL TSRRGRLENQ ETRANAIAIK ALVPLSEMFG YATVLRSNTQ
GRATFIMQFA KYEKTPKSIT EEIIKQRS
