ID E4TAD1_RIEAD Unreviewed; 598 AA.
AC E4TAD1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 ORFNames=RA0C_1398 {ECO:0000313|EMBL:AFD56295.1};
OS Riemerella anatipestifer (strain ATCC 11845 / DSM 15868 / JCM 9532 / NCTC
OS 11014).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=693978 {ECO:0000313|EMBL:AFD56295.1, ECO:0000313|Proteomes:UP000010093};
RN [1] {ECO:0000313|EMBL:AFD56295.1, ECO:0000313|Proteomes:UP000010093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15868 {ECO:0000313|Proteomes:UP000010093};
RX PubMed=22628503; DOI=10.1128/JB.00366-12;
RA Wang X., Zhu D., Wang M., Cheng A., Jia R., Zhou Y., Chen Z., Luo Q.,
RA Liu F., Wang Y., Chen X.Y.;
RT "Complete genome sequence of Riemerella anatipestifer reference strain.";
RL J. Bacteriol. 194:3270-3271(2012).
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00071}; 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; CP003388; AFD56295.1; -; Genomic_DNA.
DR RefSeq; WP_004920511.1; NC_017045.1.
DR AlphaFoldDB; E4TAD1; -.
DR GeneID; 66849749; -.
DR KEGG; rai:RA0C_1398; -.
DR KEGG; ran:Riean_1130; -.
DR PATRIC; fig|693978.17.peg.1383; -.
DR HOGENOM; CLU_009995_3_3_10; -.
DR Proteomes; UP000010093; 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; cd16260; EF4_III; 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; 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00071};
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..183
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 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 598 AA; 67180 MW; CBBFF66FE002EFD5 CRC64;
MKNIRNFCII AHIDHGKSTL ADRLLEYTNT VTQRELQAQT LDDMDLEKER GITIKSHAIQ
MDYEYKGEKY VLNLIDTPGH VDFSYEVSRS IAACEGALLI VDAAQSIQAQ TISNLYLALE
NDLEIIPVLN KIDLPSANPE EVTDEIMNLL GCEYEDVLRV SGKTGEGVHE LLEQIVERIP
APKGEPDAPL QALIFDSVYN PFRGIEAYFK VVNGKIRKGE KVKFMATDKT YEADEVGTLK
LKQQPKQEIK CGDVGYIISG IKDAREVKVG DTITSVENPA TAPIEGFEEV KPMVFAGIYP
VESEDFEELR TSLEKLRLND ASLVFEPESS AALGFGFRCG FLGMLHMEIV QERLDREFNM
NVITTVPNVS YHGYSKKEPE VPILINNPSE MMDPTVMDRV EEPYIKASII TKSDFVGAVM
TLCIEKRGEI VNQSYLTSDR VELVFNMPLA EVVFDFYDRL KSISKGYASF DYHPIGFRAS
KLVKMDILIN GDMVDALSSL IHQDNAYGIG KKMCEKLREL IPRQQFDIAV QAALGTKVIA
RETIKALRKD VTAKCYGGDI SRKRKLLEKQ KEGKKKMKQI GRVEVPQSAF MAVLKLND
//
