EFG_MYCGE
ID EFG_MYCGE Reviewed; 688 AA.
AC P47335; Q49196; Q49265; Q49303;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=MG089;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 230-458; 514-626 AND 629-688.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; L43967; AAC71307.1; -; Genomic_DNA.
DR EMBL; U01722; AAC43197.1; -; Unassigned_DNA.
DR EMBL; U02180; AAD12466.1; -; Genomic_DNA.
DR EMBL; U02136; AAD12412.1; -; Genomic_DNA.
DR PIR; H64209; H64209.
DR RefSeq; WP_009885646.1; NZ_AAGX01000002.1.
DR AlphaFoldDB; P47335; -.
DR SMR; P47335; -.
DR STRING; 243273.MG_089; -.
DR EnsemblBacteria; AAC71307; AAC71307; MG_089.
DR KEGG; mge:MG_089; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_14; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 88967at2; -.
DR BioCyc; MGEN243273:G1GJ2-101-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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_0000091156"
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:0000250"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 345..346
FT /note="NK -> KQ (in Ref. 2; AAC43197)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="N -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="S -> Y (in Ref. 2; AAD12412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 688 AA; 76539 MW; 4D906162F123B690 CRC64;
MSRTVDLKNF RNFGIMAHID AGKTTTSERI LFHSGRIHKI GETHDGESVM DWMEQEKERG
ITITSAATSV SWKNCSLNLI DTPGHVDFTV EVERSLRVLD GAIAVLDAQM GVEPQTETVW
RQASRYEVPR VIFVNKMDKT GANFERSVLS IQQRLGVKAV PIQFPIGAEN DFNGIIDIIT
KKAYFFDGNK EENAIEKPIP EQYVDQVEKL YNNLVEEVAS LDDQLMADYL DGKPIEIDAI
KNAIRNGVIH CKFFPVLCGS AFKNKGIKLL LDAVVDFLPS PVDVPPAKAI DANNKEISIK
ASDDANFIGL AFKVATDPFV GRLTFIRVYA GVLKSGSYVK NVRKNKKERV SRLVKMHAQN
RNEIDEIRAG DICAVIGLKD TTTGETLTDD KLDVQLEAMQ FAEPVISLAV EPKTKADQEK
MSIALSKLAE EDPTFKTFSD PETGQTIIAG MGELHLDILV DRMKREFKVE VNIGAPQVSF
RETFKSTSEV EGKYIKQSGG RGQYGHVKIR FEPNKDKGFE FVDKIVGGRI PREYIKPVQT
GLENAMNSGP LAGYPMIDIK ATLFDGSFHE VDSSEMAFKI AASLALKEAG KQCNPVLLEP
IMAIEVTVPE QYFGDTMGDI SSRRGIIEGT EQRDNVQLIK AKVPLKEMFG YATDLRSFSQ
GRGNYVMQFS HYAETPKSVV NEIIANKK
