ID   A6LJK6_THEM4            Unreviewed;       603 AA.
AC   A6LJK6;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
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   OrderedLocusNames=Tmel_0233 {ECO:0000313|EMBL:ABR30107.1};
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Thermosipho.
OX   NCBI_TaxID=391009 {ECO:0000313|EMBL:ABR30107.1, ECO:0000313|Proteomes:UP000001110};
RN   [1] {ECO:0000313|EMBL:ABR30107.1, ECO:0000313|Proteomes:UP000001110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429
RC   {ECO:0000313|Proteomes:UP000001110};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermosipho melanesiensis BI429.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR30107.1, ECO:0000313|Proteomes:UP000001110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429
RC   {ECO:0000313|Proteomes:UP000001110};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(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: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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000716; ABR30107.1; -; Genomic_DNA.
DR   RefSeq; WP_012056468.1; NC_009616.1.
DR   AlphaFoldDB; A6LJK6; -.
DR   STRING; 391009.Tmel_0233; -.
DR   KEGG; tme:Tmel_0233; -.
DR   eggNOG; COG0481; Bacteria.
DR   HOGENOM; CLU_009995_3_3_0; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000001110; 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   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; 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..185
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         132..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   603 AA;  67748 MW;  F9C84D751045143E CRC64;
     MKNVRNISII AHIDHGKTTL SDRILEITGA VEKRKMREQF LDSMDIERER GITIKSHPLR
     VFYKSKKNGK VYEINIVDTP GHVDFTYEVD RSLAAVEGVI LLVDASQGVQ AQTVANAYKA
     IEHNLEIIPV INKIDLPNAN IPETELEIED LIGISSEEIL KVSAKEGIGV EDVLEAIIGR
     VPSPKGTENE KLSALIFDAK YDKYRGVITY VRVFNGEIKP GDKIMTYSNK QVYEVVETGV
     FTPDMTPIEK LKAGDIGYII AGIKEVSLAK IGDTITNATD PVEEPLPGYK EIKPMVFAGM
     YPGVPEYYEE LRKALEKLKL NDSSLTFYPD HSPALGFGFR CGFLGLLHMD VVRERLEREF
     EMTVILTAPN VEYKVILKNG EEVIVNDPAK FPDESMIQEV YEPYVKLSII TPPEYLGKLM
     NLVQNEKRGI MTSTENAGFE RVVLNFEVPL AEIIFDFFDK MKASSRGYAS MDYEMIGYRK
     SELVKITILV NKEPVDALSI IAHKNKAYAM ARKLVDKLAE LIPQHQFEIP VQARAGGRII
     ARSTIKALRK DVLAKCYGGD VTRKMKLLQK QKEGKKRLRE IGSVSIPQEA FLALLKVGED
     ENK
//