ID D6ZIX6_MOBCV Unreviewed; 398 AA. AC D6ZIX6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 02-SEP-2026, entry version 80. 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}; DE EC=3.6.5.3 {ECO:0000256|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118, GN ECO:0000313|EMBL:ADI66675.1}; GN OrderedLocusNames=HMPREF0573_10356 {ECO:0000313|EMBL:ADI66675.1}; OS Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / CCUG 24716 / V125) OS (Falcivibrio vaginalis). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Actinomycetales; OC Actinomycetaceae; Mobiluncus. OX NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI66675.1, ECO:0000313|Proteomes:UP000006742}; RN [1] {ECO:0000313|Proteomes:UP000006742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43063 / DSM 2711 / V125 RC {ECO:0000313|Proteomes:UP000006742}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V., RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G., RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A., RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RT "Complete sequence of Mobiluncus curtisii ATCC 43063."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTP hydrolase that promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; CC Evidence={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; CP001992; ADI66675.1; -; Genomic_DNA. DR RefSeq; WP_004008360.1; NC_014246.1. DR AlphaFoldDB; D6ZIX6; -. DR STRING; 548479.HMPREF0573_10356; -. DR GeneID; 55564511; -. DR KEGG; mcu:HMPREF0573_10356; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_11; -. DR Proteomes; UP000006742; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. 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 FunFam; 2.40.30.10:FF:000001; Elongation factor Tu; 1. DR FunFam; 3.40.50.300:FF:000003; Elongation factor Tu; 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; IPR050055; EF-Tu_GTPase. 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. 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; NF000766; PRK00049.1; 1. DR NCBIfam; NF009372; PRK12735.1; 1. DR NCBIfam; NF009373; PRK12736.1; 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|ARBA:ARBA00022490, 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00118}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00118}; KW Metal-binding {ECO:0000256|HAMAP-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}; Reference proteome {ECO:0000313|Proteomes:UP000006742}. FT DOMAIN 10..208 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT REGION 19..26 FT /note="G1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 64..68 FT /note="G2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 85..88 FT /note="G3" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 140..143 FT /note="G4" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 178..180 FT /note="G5" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 26 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 85..89 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 140..143 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 398 AA; 43814 MW; 91B8D1A4EDA23572 CRC64; MAQGTYTHDK PHVNVGTIGH VDHGKTTLTA AITKVLADKY PDLPANKFTP FDQVDNAPEE RQRGITINVS HVEYETPNRH YAHVDAPGHA DYIKNMITGA AQMDGAILVV AATDGPMAQT KEHILLAKQV GVPSILVALN KCDSSDVDED MLEIVEDEIR DDLEKQGFDR DCPIIHVSAL KALEGDPEWT KKIEELMEAV DTYIPEPVRD LDKPFLMPIE DVFTITGRGT VVTGRVERGK LPLNAEVEIV GIRPTQKTTV TGIEMFHKSM DEAYAGENCG LLLRGTKRED VERGQVVCIP GSVTPHTKFE GKVYILKKDE GGRHKSFYDG YRPQFFFRTT DVTGVIHLPE GTEMVMPGDT TEISVELIQP IAMEEGLGFA IREGGRTVGS GKVTKIIA //