ID   D8JES9_ACISD            Unreviewed;       396 AA.
AC   D8JES9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=AOLE_15370 {ECO:0000313|EMBL:ADI91961.1}, AOLE_18035
GN   {ECO:0000313|EMBL:ADI92491.1};
OS   Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI91961.1, ECO:0000313|Proteomes:UP000000392};
RN   [1] {ECO:0000313|EMBL:ADI91961.1, ECO:0000313|Proteomes:UP000000392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DR1 {ECO:0000313|EMBL:ADI91961.1}, and JCM 16667 / KCTC 23045 /
RC   DR1 {ECO:0000313|Proteomes:UP000000392};
RX   PubMed=20639327; DOI=10.1128/JB.00722-10;
RA   Jung J., Baek J.H., Park W.;
RT   "Complete genome sequence of the diesel-degrading Acinetobacter sp. strain
RT   DR1.";
RL   J. Bacteriol. 192:4794-4795(2010).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
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DR   EMBL; CP002080; ADI91961.1; -; Genomic_DNA.
DR   EMBL; CP002080; ADI92491.1; -; Genomic_DNA.
DR   RefSeq; WP_004794160.1; NC_014259.1.
DR   AlphaFoldDB; D8JES9; -.
DR   GeneID; 9384048; -.
DR   KEGG; acd:AOLE_15370; -.
DR   KEGG; acd:AOLE_18035; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_2_6; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000000392; 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 {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}.
FT   DOMAIN          10..206
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   396 AA;  42881 MW;  CF3FE73D53D26C76 CRC64;
     MAKAKFERNK PHVNVGTIGH VDHGKTTLTA AIATICAKTY GGEAKDYSQI DSAPEEKARG
     ITINTSHVEY DSPIRHYAHV DCPGHADYVK NMITGAAQMD GAILVCAATD GPMPQTREHI
     LLSRQVGVPY IIVFLNKCDL VDDEELLELV EMEVRELLST YDFPGDDTPV IRGSALAALN
     GDAGQYGESS VLALVEALDS YIPEPERAID KAFLMPIEDV FSISGRGTVV TGRVEAGIVK
     VGEEVEIVGI KDTVKTTVTG VEMFRKLLDE GRAGENCGVL LRGTKREDVQ RGQVLAKPGT
     IKPHTKFDAE VYVLSKEEGG RHTPFLNGYR PQFYFRTTDV TGAIQLQDGV EMVMPGDNVE
     MSVELIHPIA MDPGLRFAIR EGGRTVGAGV VAKVTA
//