LEPA_MYCFP
ID LEPA_MYCFP Reviewed; 599 AA.
AC Q8GCP5; C4XEU4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=MBIO_0401;
OS Mycoplasmopsis fermentans (strain ATCC 19989 / NBRC 14854 / NCTC 10117 /
OS PG18) (Mycoplasma fermentans).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=496833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18;
RX PubMed=12446643; DOI=10.1128/jb.184.24.6929-6941.2002;
RA Calcutt M.J., Lewis M.S., Wise K.S.;
RT "Molecular genetic analysis of ICEF, an integrative conjugal element that
RT is present as a repetitive sequence in the chromosome of Mycoplasma
RT fermentans PG18.";
RL J. Bacteriol. 184:6929-6941(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18;
RX PubMed=19219498; DOI=10.1007/s00284-009-9362-6;
RA Ishida N., Irikura D., Matsuda K., Sato S., Sone T., Tanaka M., Asano K.;
RT "Molecular cloning and expression of a novel cholinephosphotransferase
RT involved in glycoglycerophospholipid biosynthesis of Mycoplasma
RT fermentans.";
RL Curr. Microbiol. 58:535-540(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH69666.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY168953; AAN85212.1; -; Genomic_DNA.
DR EMBL; AP009608; BAH69666.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_013354583.1; NC_021002.1.
DR AlphaFoldDB; Q8GCP5; -.
DR SMR; Q8GCP5; -.
DR STRING; 496833.MBIO_0401; -.
DR EnsemblBacteria; BAH69666; BAH69666; MBIO_0401.
DR KEGG; mfp:MBIO_0401; -.
DR PATRIC; fig|496833.3.peg.829; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_14; -.
DR OrthoDB; 182107at2; -.
DR Proteomes; UP000006810; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
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..599
FT /note="Elongation factor 4"
FT /id="PRO_0000176296"
FT DOMAIN 4..181
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 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 599 AA; 67683 MW; BA09E300F9BE65D0 CRC64;
MDKSKIRNFS IIAHIDHGKS TLADRILEIT NTVSDHDMDD QFLDQMDLER ERGITIKLNA
VQIKYKDYVF HLIDTPGHVD FTYEVSRSLA ASEGALLLVD ATQGIEAQTL ANVYLALENN
LTIIPIINKI DLPSADIEAT KNEIEEVIGL PTDNAVCISA KTGLNCEAVL AAIEKYIPAP
KDADDSKPLK ALIFDSYFDE YRGVVMLIRI FEGELKVGDE FMFMSNGQRY FVSELGVRSP
KETKKKRLEA GEVGYVAATI RDAREVSVGD TITLVNRPAE KALPGYKKKK PVLYTGFYPI
DTRDYMELKE SLEKIALSDS SITWEQETSK ALGFGFRVGF LGMLHMEILQ ERLNREYKIG
IIATSPSVEY DVHMTDGSIK KISNPALLPD RTFIDHIDEP YIKAEILVPN EYIGNVMELC
QNKRGIYINM DYIDANRSRL IYEMPLGEII FDFFDRLKSL TKGYASFEYD LIGYKTSDLV
KVDILLNGDK IDAFSIITHK DSAYSKARDL TQKLKEAIPR QNFEVPVQAT IGSKIIARET
IKAYRKDVTS KLHAADVSRY KKLLEKQKAG KKKMKMLGTV EVPQEAFLSI LKTNIDKKK
