LEPA_MYCGE
ID LEPA_MYCGE Reviewed; 598 AA.
AC P47384; Q49264; Q49477;
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 4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071};
DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071};
GN Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071}; OrderedLocusNames=MG138;
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 109-197.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=1945886; DOI=10.1093/nar/19.21.6027;
RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A random sequencing approach for placing markers on the physical map of
RT Mycoplasma genitalium.";
RL Nucleic Acids Res. 19:6027-6031(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-413 AND 440-598.
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: Required for accurate and efficient protein synthesis under
CC certain stress conditions. May act as a fidelity factor of the
CC translation reaction, by catalyzing a one-codon backward translocation
CC of tRNAs on improperly translocated ribosomes. Back-translocation
CC proceeds from a post-translocation (POST) complex to a pre-
CC translocation (PRE) complex, thus giving elongation factor G a second
CC chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-
CC dependent manner. {ECO:0000255|HAMAP-Rule:MF_00071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00071};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00071};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00071};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00071}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00071}.
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DR EMBL; L43967; AAC71355.1; -; Genomic_DNA.
DR EMBL; X61521; CAB97511.1; -; Genomic_DNA.
DR EMBL; U01745; AAD10558.1; -; Genomic_DNA.
DR EMBL; U02133; AAD12410.1; -; Genomic_DNA.
DR PIR; C64215; C64215.
DR RefSeq; WP_010869350.1; NC_000908.2.
DR AlphaFoldDB; P47384; -.
DR SMR; P47384; -.
DR STRING; 243273.MG_138; -.
DR EnsemblBacteria; AAC71355; AAC71355; MG_138.
DR KEGG; mge:MG_138; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_14; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 182107at2; -.
DR BioCyc; MGEN243273:G1GJ2-152-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.2570; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR035654; LepA_IV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43512; PTHR43512; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR01393; lepA; 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 Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..598
FT /note="Elongation factor 4"
FT /id="PRO_0000176298"
FT DOMAIN 4..185
FT /note="tr-type G"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT CONFLICT 413
FT /note="D -> G (in Ref. 3; AAD12410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 67937 MW; C16F1864E24C941D CRC64;
MEQKNIRNFS IIAHIDHGKS TLSDRLLEHS LGFEKRLLQA QMLDTMEIER ERGITIKLNA
VELKINVDNN NYLFHLIDTP GHVDFTYEVS RSLAACEGVL LLVDATQGIQ AQTISNAYLA
LENNLEIIPV INKIDMDNAD IETTKDSLHN LLGVEKNSIC LVSAKANLGI DQLIQTIIAK
IPPPKGEINR PLKALLFDSY YDPYKGVVCF IRVFDGCLKV NDKVRFIKSN SVYQIVELGV
KTPFFEKRDQ LQAGDVGWFS AGIKKLRDVG VGDTIVSFDD QFTKPLAGYK KILPMIYCGL
YPVDNSDYQN LKLAMEKIII SDAALEYEYE TSQALGFGVR CGFLGLLHMD VIKERLEREY
NLKLISAPPS VVYKVLLTNG KEISIDNPSL LPERSKIKAI SEPFVKVFID LPDQYLGSVI
DLCQNFRGQY ESLNEIDINR KRICYLMPLG EIIYSFFDKL KSISKGYASL NYEFYNYQHS
QLEKVEIMLN KQKIDALSFI SHKDFAFKRA KKFCTKLKEL IPKHLFEIPI QATIGSKVIA
RETIKAVRKD VIAKLYGGDV SRKKKLLEKQ KEGKKRLKAV GSVQLPQELF SHLLKDED
