ID B0VMA6_ACIBS Unreviewed; 396 AA. AC B0VMA6; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 111. 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=tufB {ECO:0000313|EMBL:CAP02520.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufA GN {ECO:0000313|EMBL:CAP01877.1}; GN OrderedLocusNames=ABSDF2567 {ECO:0000313|EMBL:CAP01877.1}, ABSDF3250 GN {ECO:0000313|EMBL:CAP02520.1}; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP02520.1, ECO:0000313|Proteomes:UP000001741}; RN [1] {ECO:0000313|EMBL:CAP02520.1, ECO:0000313|Proteomes:UP000001741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF {ECO:0000313|EMBL:CAP02520.1, RC ECO:0000313|Proteomes:UP000001741}; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., RA Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). RN [2] {ECO:0000313|EMBL:CAP02520.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SDF {ECO:0000313|EMBL:CAP02520.1}; RA Genoscope - CEA; RL Submitted (FEB-2008) 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: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}. 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; CU468230; CAP01877.1; -; Genomic_DNA. DR EMBL; CU468230; CAP02520.1; -; Genomic_DNA. DR AlphaFoldDB; B0VMA6; -. DR SMR; B0VMA6; -. DR KEGG; abm:ABSDF2567; -. DR KEGG; abm:ABSDF3250; -. DR HOGENOM; CLU_007265_0_0_6; -. DR Proteomes; UP000001741; 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; 42892 MW; 56B9D9300174DF8A CRC64; MAKAKFERNK PHVNVGTIGH VDHGKTTLTA AIATICAKTY GGEAKDYSQI DSAPEEKARG ITINTSHVEY DSPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVCAATD GPMPQTREHI LLSRQVGVPY IIVFLNKCDL VDDEELLELV EMEVRELLST YDFPGDDTPV IRGSALAALN GEAGPYGEES VLALVAALDS YIPEPERAID KAFLMPIEDV FSISGRGTVV TGRVEAGIIK VGEEVEIVGI KDTVKTTVTG VEMFRKLLDE GRAGENCGIL LRGTKREEVQ RGQVLAKPGT IKPHTKFDAE VYVLSKEEGG RHTPFLNGYR PQFYFRTTDV TGAIQLKEGV EMVMPGDNVE MSVELIHPIA MDPGLRFAIR EGGRTVGAGV VAKVTA //