ID F0J0K3_ACIMA Unreviewed; 395 AA. AC F0J0K3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 67. 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 ECO:0000313|EMBL:BAJ81539.1}; GN OrderedLocusNames=ACMV_21920 {ECO:0000313|EMBL:BAJ81539.1}; GN ORFNames=Apmu_0006_11 {ECO:0000313|EMBL:GAN72499.1}; OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU OS 301). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ81539.1, ECO:0000313|Proteomes:UP000007100}; RN [1] {ECO:0000313|EMBL:BAJ81539.1, ECO:0000313|Proteomes:UP000007100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AIU301 {ECO:0000313|EMBL:BAJ81539.1}, and DSM 11245 / JCM 8867 RC / AIU301 {ECO:0000313|Proteomes:UP000007100}; RA Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H., RA Hosoyama A., Yamada R., Fujita N.; RT "Whole genome sequence of Acidiphilium multivorum AIU301."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GAN72499.1, ECO:0000313|Proteomes:UP000032662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AIU301 {ECO:0000313|EMBL:GAN72499.1, RC ECO:0000313|Proteomes:UP000032662}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Acidiphilium multivorum AIU301."; RL Submitted (NOV-2012) 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; AP012035; BAJ81539.1; -; Genomic_DNA. DR EMBL; BANA01000006; GAN72499.1; -; Genomic_DNA. DR RefSeq; WP_007424171.1; NZ_BANA01000006.1. DR AlphaFoldDB; F0J0K3; -. DR SMR; F0J0K3; -. DR KEGG; amv:ACMV_21920; -. DR HOGENOM; CLU_007265_0_1_5; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000007100; Chromosome. DR Proteomes; UP000032662; Unassembled WGS sequence. 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..205 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 395 AA; 42629 MW; FD720A13AA0C62FD CRC64; MAKAKFERTK PHCNIGTIGH VDHGKTSLTA AITKVLAESG GATFRAYDSI DAAPEERARG ITIATAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLARQVGVPA LVVFLNKMDM ADPDLVELVE MEVRDLLSKY EFPGDDIPII KGSALCALED SNAELGREAI LKLMEAVDSY IPQPERPKDK PFLMPVEDVF SISGRGTVVT GRVERGIIKV GDEVEIVGLK ATVKTTVTGV EMFRKLLDQG EAGDNIGALL RGTKREDVER GQVLAAPGSI TPHTNFSGSV YILNKEEGGR HTPFFTNYRP QFYFRTTDVT GVVTLPEGVE MVMPGDNVTV SVELIAPIAM DEGLRFAIRE GGRTVGSGVV ASITK //