ID F0TDZ2_LACAM Unreviewed; 396 AA. AC F0TDZ2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 64. 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:MDB6257129.1}; GN OrderedLocusNames=LAC30SC_04240 {ECO:0000313|EMBL:ADZ07013.1}; GN ORFNames=ODU72_00280 {ECO:0000313|EMBL:MDB6257129.1}, ODV15_04160 GN {ECO:0000313|EMBL:MDB6261762.1}; OS Lactobacillus amylovorus. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1604 {ECO:0000313|EMBL:ADZ07013.1, ECO:0000313|Proteomes:UP000007491}; RN [1] {ECO:0000313|EMBL:ADZ07013.1, ECO:0000313|Proteomes:UP000007491} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=30SC {ECO:0000313|EMBL:ADZ07013.1, RC ECO:0000313|Proteomes:UP000007491}; RX PubMed=21478365; DOI=10.1128/JB.00343-11; RA Oh S., Roh H., Ko H.J., Kim S., Kim K.H., Lee S.E., Chang I.S., Kim S., RA Choi I.G.; RT "Complete genome sequencing of Lactobacillus acidophilus 30SC, isolated RT from swine intestine."; RL J. Bacteriol. 193:2882-2883(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=30SC; RA Roh H., Ko H.-J., Kim S.-H., Choi I.-G., Oh S.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:MDB6257129.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M356A {ECO:0000313|EMBL:MDB6261762.1}, and M490A RC {ECO:0000313|EMBL:MDB6257129.1}; RX PubMed=36677394; RA Moravkova M., Kostovova I., Kavanova K., Pechar R., Stanek S., Brychta A., RA Zeman M., Kubasova T.; RT "Antibiotic Susceptibility, Resistance Gene Determinants and Corresponding RT Genomic Regions in Lactobacillus amylovorus Isolates Derived from Wild RT Boars and Domestic Pigs."; RL Microorganisms 11:0-0(2022). RN [4] {ECO:0000313|EMBL:MDB6257129.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M356A {ECO:0000313|EMBL:MDB6261762.1}, and M490A RC {ECO:0000313|EMBL:MDB6257129.1}; RA Kostovova I., Moravkova M., Pechar R.; RL Submitted (OCT-2022) 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; CP002559; ADZ07013.1; -; Genomic_DNA. DR EMBL; JAOTGY010000001; MDB6257129.1; -; Genomic_DNA. DR EMBL; JAOTGU010000004; MDB6261762.1; -; Genomic_DNA. DR RefSeq; WP_013437664.1; NZ_JAOTHM010000007.1. DR AlphaFoldDB; F0TDZ2; -. DR STRING; 1604.LAC30SC_04240; -. DR KEGG; lai:LAC30SC_04240; -. DR HOGENOM; CLU_007265_0_1_9; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000007491; Chromosome. DR Proteomes; UP001141981; Unassembled WGS sequence. DR Proteomes; UP001143700; 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: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}; Hydrolase {ECO:0000313|EMBL:ADZ07013.1}; 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 11..205 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 20..27 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 82..86 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 137..140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 396 AA; 43590 MW; E602B747E98352C4 CRC64; MAEKEHYVRT KPHVNIGTIG HVDHGKTTLT AAITTVLAEK GLAKAEDYSQ IDAAPEEKER GITINTAHVE YETENRHYAH MDAPGHADYI KNMITGAAQM DGAILVVAAT DGPMPQTREH ILLARQVGVN YIVVFLNKCD LVDDPELIDL VEMEVRDLLT EYDYPGDDIP VVRGSALKAL QGDKEAQEQI LKLMDIVDEY IPTPERQTDK PFLMPVEDVF TITGRGTVAS GRIDRGTVKI GDEVEIVGLV DKVLKSVVTG LEMFHKTLDL GEAGDNVGVL LRGIDRDQVV RGQVLAAPGS IQTHEKFKGQ VYVLKKDEGG RHTPFFSDYR PQFYFHTTDI TGEIELPEGT EMVMPGDNTE FTVTLIKPAA IEKGTKFTIR EGGRTVGAGQ VTEILD //