ID W8GN80_9MOLU Unreviewed; 599 AA.
AC W8GN80;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:AHK22471.1};
GN ORFNames=X271_00365 {ECO:0000313|EMBL:AHK22471.1};
OS Candidatus Hepatoplasma crinochetorum Av.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Hepatoplasma.
OX NCBI_TaxID=1427984 {ECO:0000313|EMBL:AHK22471.1, ECO:0000313|Proteomes:UP000019450};
RN [1] {ECO:0000313|EMBL:AHK22471.1, ECO:0000313|Proteomes:UP000019450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Av {ECO:0000313|EMBL:AHK22471.1,
RC ECO:0000313|Proteomes:UP000019450};
RX PubMed=24482531; DOI=10.1093/gbe/evu020;
RA Leclercq S., Dittmer J., Bouchon D., Cordaux R.;
RT "Phylogenomics of "Candidatus Hepatoplasma crinochetorum," a Lineage of
RT Mollicutes Associated with Noninsect Arthropods.";
RL Genome Biol. Evol. 6:407-415(2014).
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; CP006932; AHK22471.1; -; Genomic_DNA.
DR AlphaFoldDB; W8GN80; -.
DR STRING; 1427984.X271_00365; -.
DR KEGG; hcr:X271_00365; -.
DR PATRIC; fig|1427984.3.peg.352; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_14; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000019450; 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; 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; 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 SMART; SM00838; EFG_C; 1.
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 Elongation factor {ECO:0000313|EMBL:AHK22471.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019450}.
FT DOMAIN 4..185
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 599 AA; 68022 MW; 14C8322740E821DF CRC64;
MKKENIRNFA IIAHIDHGKS TLADRILEFT HSVTKREIHN QMLDTMDLER ERGITIKLNA
VQIEYQYQNQ IYQLNLIDTP GHVDFTYEVS RSLAASEGAI LLVDATQGVQ PQTIANLYLA
IENDLKIIPV INKIDSENAN ILKTKQEIKE ILGIDASDAP LISAKTGKNI EEVLIKIIND
IPPPLNADDN LPLKGLVFDA YFDSYQGVIL FVKIFQGFIT KNQKLTFIQS KTDLDVISVG
VNTPKEKVKE KLNAGETGWI ITNIKDIKKI SIGDTLTTRE NKDKIKALPG YRPSKPMVFS
GFYPLDTEKY QGLEEALDKI SLSDSSLSYE KENSKALGFG FRVGFLGLLH LEIIQERIER
EFKIPVIATI PSVIYKVTLT NKKIKYIQNP VDFPDKSYIL QIEEPYVKVT IYSPENYMGK
LIEYVHSKRG IYQNLEIYSE KMNALIYHLP LGEIVFDFFN AVKSISKGYA SFDYEQIGYQ
KGDLVKLDFL IAKEQVDAFS RIVDRKNAYQ IAKVMVEKLK EIVPRQNFEI AIQAVIGGKV
IARETVKAYR KDVTGYLYGG DVSRKKKLLE KQKKGKKKMK QIGSVTLPKN AFIDVLKTK
//
