ID G2NE18_STREK Unreviewed; 624 AA.
AC G2NE18;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=SACTE_1973 {ECO:0000313|EMBL:AEN09878.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN09878.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN09878.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN09878.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(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; CP002993; AEN09878.1; -; Genomic_DNA.
DR AlphaFoldDB; G2NE18; -.
DR STRING; 862751.SACTE_1973; -.
DR KEGG; ssx:SACTE_1973; -.
DR PATRIC; fig|862751.12.peg.2054; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_11; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000001397; 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; 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 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:UP000001397}.
FT DOMAIN 17..203
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 29..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 150..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 624 AA; 68685 MW; E1B525930E5B87FC CRC64;
MPATPTHVPE PSRTDPALIR NFCIIAHIDH GKSTLADRML QLTGVVDQRQ MRAQYLDRMD
IERERGITIK SQAVRLPWAP NEGEDQGKTH ILNMIDTPGH VDFTYEVSRS LAACEGTILL
VDAAQGIEAQ TLANLYLAME NDLTIVPVLN KIDLPAAQPE KFSEELANLI GCRPEDVLKV
SAKTGVGVDA LLDRVVRDIP APVGQADAAA RAMIFDSVYD PYRGVVTYVR VVDGQLNKRE
RIRMMSTGAT HELLEIGVSS PEMTPADGIG VGEVGYIITG VKDVRQSKVG DTITSLSNGA
TEALGGYKDP KPMVFSGLYP LDGSDYPDLR EALDKLQLND AALVYEPETS AALGFGFRVG
FLGLLHLDVI RERLEREFGL ELIATAPNVV YRVEMEDGTE HTVTNPSEFP EGKIDKVHEP
VVRATVLAPS EFIGAIMELC QNRRGTLLGM DYLSEDRVEI RYTLPLAEIV FDFFDQLKSK
TRGYASLDYE PTGEQAAQLV KVDILLHGDK VDAFSAVTHK DKAYAYGVRL VAKLQKLIPR
QNFEVPIQAA IGSRVIARET VRAIRKDVLA KCYGGDISRK RKLLEKQKEG KKRMKMVGNV
EVPQDAFISV LSTDESAGEG KGKK
//
