ID EFTU_BUCAI Reviewed; 394 AA.
AC O31297; Q9AQA1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA;
GN OrderedLocusNames=BU526;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-384.
RX PubMed=9580987; DOI=10.1093/oxfordjournals.molbev.a025958;
RA Brynnel E.U., Kurland C.G., Moran N.A., Andersson S.G.;
RT "Evolutionary rates for tuf genes in endosymbionts of aphids.";
RL Mol. Biol. Evol. 15:574-582(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-313.
RA Wernegreen J.J., Moran N.A.;
RT "Accelerated evolutionary rates at biosynthetic loci of Buchnera-
RT Uroleucon.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000003; BAB13219.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y12307; CAA72974.1; -; Genomic_DNA.
DR EMBL; AF217552; AAK01023.1; -; Genomic_DNA.
DR RefSeq; NP_240333.2; NC_002528.1.
DR RefSeq; WP_009874477.1; NC_002528.1.
DR AlphaFoldDB; O31297; -.
DR SMR; O31297; -.
DR STRING; 563178.BUAP5A_519; -.
DR EnsemblBacteria; BAB13219; BAB13219; BAB13219.
DR KEGG; buc:BU526; -.
DR PATRIC; fig|107806.10.peg.531; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_2_6; -.
DR Proteomes; UP000001806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR CDD; cd03707; EFTU_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
DR InterPro; IPR031157; G_TR_CS.
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 InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00485; EF-Tu; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
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 Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..394
FT /note="Elongation factor Tu"
FT /id="PRO_0000091296"
FT DOMAIN 10..204
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 60..64
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 136..139
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 174..176
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT CONFLICT 89
FT /note="I -> M (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 43465 MW; 09B73EADCA0DF5F6 CRC64;
MSKEKFQRLK PHINVGTIGH VDHGKTTLTA AITTVLSKKF GGSARAFDQI DNAPEEKARG
ITINTSHVEY DTEFRHYAHV DCPGHADYIK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRDLLTQ YDFPGDDTPI IRGSALKALE
GDPEWESKII DLSKFLDSYI PEPKRAVDQP FLLPIEDVFS ISGRGTVVTG RVEKGIIKVG
EEVEIVGIKK TTKTTCTGVE MFRKLLDEGR AGENVGVLLR GTKRDEIERG QVLAKPGSIH
PHTTFESEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDVTG SIELPEGIEM VMPGDNIKMT
VTLINPIAMA DGLRFAIREG GRTVGAGVVS KVLL
//
