ID EFG_MESFL Reviewed; 689 AA.
AC Q6F0J4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=Mfl622;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Entomoplasmataceae; Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE017263; AAT75979.1; -; Genomic_DNA.
DR RefSeq; WP_011183519.1; NC_006055.1.
DR RefSeq; YP_053863.1; NC_006055.1.
DR AlphaFoldDB; Q6F0J4; -.
DR SMR; Q6F0J4; -.
DR STRING; 265311.Mfl622; -.
DR PaxDb; 265311-Mfl622; -.
DR EnsemblBacteria; AAT75979; AAT75979; Mfl622.
DR GeneID; 2897751; -.
DR KEGG; mfl:Mfl622; -.
DR PATRIC; fig|265311.5.peg.625; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_14; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000006647; 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; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04088; EFG_mtEFG_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 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..689
FT /note="Elongation factor G"
FT /id="PRO_0000091150"
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 689 AA; 76130 MW; F531F06FEBAF882F CRC64;
MPREFSLENT RNLGIMAHID AGKTTTTERI LFHTGKIHKI GETHEGASQM DWMAQEQERG
ITITSAATTA FWKNNRFNII DTPGHVDFTV EVERSLRVLD GAVAVLDGQS GVEPQTETVW
RQATTYRVPR IVFVNKMDKT GADFIYSVKS IGDRLGAKAA PIQLPIGAED NFTGIIDLVE
MKAYEFDGKA EEIAKEIEIP ADLKDQAEIL RSELVEAAVE YDEELMMKFL DGEEITIPEL
KQAIRKGVIG AEFFPVLAGS AFKNKGVKLL LDAVVDYLPS PLDVPSIKGV LPNGEEAERH
ADDNEPFSAL AFKVMTDPFV GKLTFFRVYS GILTKGSYVL NSTKGDKERV GRILQMHANN
RNEIEEVYAG DIAAAVGLKN TTTGDTLVDE KHEIILESMV FPEPVIQLAL EPKTKADQEK
MGLALSKLAE EDPTFRTYTD EETGQTIIAG MGELHLDIIV DRMRREFKVE TNVGAPQVSY
RETIKLPAKA EGKYVKQSGG RGSYGHVVIE FEPNVDKGFE WVDKITGGRV SKEYINAARV
GLENALTNGV VAGYPMIDVK ATIVDGSMHD VDSNEMAYKI AASFALKEAC KKMNPVILEP
IMNVEVTVPD EYYGDVMGNI SSKRGLIEGS EQRGNAQTIK SKVPLTEMFG YATELRSFTQ
GRGNYTMIFS HYAEAPRSIA EEIIKKSGK
//
