ID F6FHR2_MYCHI Unreviewed; 590 AA.
AC F6FHR2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Elongation factor 4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_00071};
DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000256|HAMAP-Rule:MF_00071};
GN Name=lepA {ECO:0000256|HAMAP-Rule:MF_00071,
GN ECO:0000313|EMBL:AEG73826.1};
GN OrderedLocusNames=MHF_1596 {ECO:0000313|EMBL:AEG73826.1};
OS Mycoplasma haemofelis (strain Ohio2).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=859194 {ECO:0000313|EMBL:AEG73826.1, ECO:0000313|Proteomes:UP000007952};
RN [1] {ECO:0000313|EMBL:AEG73826.1, ECO:0000313|Proteomes:UP000007952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ohio2 {ECO:0000313|EMBL:AEG73826.1,
RC ECO:0000313|Proteomes:UP000007952};
RX PubMed=21317328; DOI=10.1128/JB.00133-11;
RA Messick J.B., Santos A.P., Guimaraes A.M.;
RT "Complete genome sequences of two hemotropic Mycoplasmas, Mycoplasma
RT haemofelis strain Ohio2 and Mycoplasma suis strain Illinois.";
RL J. Bacteriol. 193:2068-2069(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ohio2;
RA Santos A.P., Guimaraes A.M.S., SanMiguel P.J., Martin S.W., Messick J.B.;
RT "The Genome of Mycoplasma haemofelis Strain Ohio2, a pathogenic hemoplasma
RT of the cat.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00071};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00071};
CC Cytoplasmic side {ECO:0000256|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:0000256|ARBA:ARBA00005454, ECO:0000256|HAMAP-Rule:MF_00071}.
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DR EMBL; CP002808; AEG73826.1; -; Genomic_DNA.
DR AlphaFoldDB; F6FHR2; -.
DR STRING; 859194.MHF_1596; -.
DR KEGG; mhf:MHF_1596; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_14; -.
DR BioCyc; MHAE859194:G1GR7-1598-MONOMER; -.
DR Proteomes; UP000007952; 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; cd03699; EF4_II; 1.
DR CDD; cd01890; LepA; 1.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 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_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 NCBIfam; TIGR01393; lepA; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 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 SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00071};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00071};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00071}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071}.
FT DOMAIN 2..180
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 14..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 590 AA; 66254 MW; 95C3FB5069B8D2F1 CRC64;
MSSIKNFCII AHIDHGKSTL SDRIIEMTSN ISEREMRPQI LDSMDLERER GITIKLNAVR
LQYKDIQLNL IDTPGHADFS YEVSRSLSAC EGAILVIDAT KGVQAQTVSN YFLAKKANLE
IVVAINKIDI PSINLDDVKT QIRNKLGLDP EEAVHISAKT GLGVDKLLEV VSRKVPDSPN
LLNEPLKALI FDSYYDPFKG AIVFIRVFGG SLKKGSKIKF IQTGKVSDVI ELGIKTPKME
NVDELSSGEV GWVNANIKNL KEIRVGDTIT LVDFPCDQPC SGYSEVLPMV YSSFFALESE
KQNLFKQAIE KISLSDGSFV YQYEPSAALG FGCRCGFLGL LHLEIIKERL FREHSISVIV
TNPTVKYEVV LTSGDSIFLT SPSDLPDLSK IKAIKEPYVL ASISVSKEFI GKIIELMEKY
RAQYVDLNYL SEDQAVLKYE IPLSEIIQDF YDAIKTLTHG YGSMDYELLD YRESKLVKVD
ILLNGVIAPL FSFITDSSQA YRKGKNLVEK LKECISPHLF EISIQAAINN KVISRENIKA
LRKHVTAKCY GGDITRKKKL WERQKEGKKK MKQIGKVTLP PDIFEKILRN
//
