ID   EFTU_ACIAD              Reviewed;         396 AA.
AC   Q6FF97; Q6FDS5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE   AltName: Full=EF-Tu 1;
GN   Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufB;
GN   OrderedLocusNames=ACIAD0299;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA;
GN   OrderedLocusNames=ACIAD0885;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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=CAG67783.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR543861; CAG67260.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG67783.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004922118.1; NC_005966.1.
DR   AlphaFoldDB; Q6FF97; -.
DR   SMR; Q6FF97; -.
DR   STRING; 62977.ACIAD0299; -.
DR   PRIDE; Q6FF97; -.
DR   EnsemblBacteria; CAG67260; CAG67260; ACIAD0299.
DR   EnsemblBacteria; CAG67783; CAG67783; ACIAD0885.
DR   GeneID; 45233345; -.
DR   KEGG; aci:ACIAD0299; -.
DR   KEGG; aci:ACIAD0885; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_2_6; -.
DR   OrthoDB; 621774at2; -.
DR   BioCyc; ASP62977:ACIAD_RS01420-MON; -.
DR   BioCyc; ASP62977:ACIAD_RS04085-MON; -.
DR   Proteomes; UP000000430; 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:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 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..396
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000337302"
FT   DOMAIN          10..206
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"
SQ   SEQUENCE   396 AA;  42955 MW;  51C4442B84266E7B CRC64;
     MAKAKFERNK PHVNVGTIGH VDHGKTTLTA AIATICAKTY GGEAKDYSQI DSAPEEKARG
     ITINTSHVEY DSPIRHYAHV DCPGHADYVK NMITGAAQMD GAILVCAATD GPMPQTREHI
     LLSRQVGVPY IVVFLNKCDL VDDEELLELV EMEVRELLST YDFPGDDTPV IRGSALKALE
     GDAGQYGESS VLALVEALDT YIPEPERAID KAFLMPIEDV FSISGRGTVV TGRVEAGIVK
     VGESVEIVGI RDTQTTTVTG VEMFRKLLDE GRAGENCGVL LRGTKREDVQ RGQVLAKPGT
     IKPHTKFDAE VYVLSKEEGG RHTPFLNGYR PQFYFRTTDV TGAIQLKEGV EMVMPGDNVE
     MSVELIHPIA MDPGLRFAIR EGGRTVGAGV VAKVTA