ID C8XCG1_NAKMY Unreviewed; 396 AA. AC C8XCG1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 27-MAR-2024, 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}; GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Namu_1119 {ECO:0000313|EMBL:ACV77526.1}; OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM OS 9543 / NBRC 105858 / Y-104) (Microsphaera multipartita). OC Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae; OC Nakamurella. OX NCBI_TaxID=479431 {ECO:0000313|EMBL:ACV77526.1, ECO:0000313|Proteomes:UP000002218}; RN [1] {ECO:0000313|Proteomes:UP000002218} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 / RC Y-104 {ECO:0000313|Proteomes:UP000002218}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Ovchinnikova G., Sims D., Meincke L., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Klenk H.-P., Eisen J.A.; RT "The complete genome of Nakamurella multipartita DSM 44233."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACV77526.1, ECO:0000313|Proteomes:UP000002218} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 / RC Y-104 {ECO:0000313|Proteomes:UP000002218}; RX PubMed=21304699; RA Tice H., Mayilraj S., Sims D., Lapidus A., Nolan M., Lucas S., RA Glavina Del Rio T., Copeland A., Cheng J.F., Meincke L., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Chen F.; RT "Complete genome sequence of Nakamurella multipartita type strain (Y- RT 104)."; RL Stand. Genomic Sci. 2:168-175(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}. 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; CP001737; ACV77526.1; -; Genomic_DNA. DR RefSeq; WP_015746440.1; NC_013235.1. DR AlphaFoldDB; C8XCG1; -. DR STRING; 479431.Namu_1119; -. DR KEGG; nml:Namu_1119; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_11; -. DR InParanoid; C8XCG1; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000002218; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000002218}. 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 83..87 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 138..141 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 396 AA; 43449 MW; 41B612B60231203B CRC64; MAKAKFDRSK PHVNIGTIGH VDHGKTTLTA AITKVLADKY PTLNQASAFD QIDKAPEERQ RGITINIAHV EYQTEKRHYA HVDAPGHADY IKNMITGAAQ MDGAILVVAA TDGPMPQTKE HVLLARQVGV PYILVALNKS DMVDDEEILE LVELEVRELL AGQDFDEDAP VIRTSGLKAL EGDPEWVKTV EDLMDAVDES IPEPERDTDK PFLMPIEDVF TITGRGTVVT GKVERGVINV NATVEIVGIK PKSFQTTVTG IEMFRKLLDT AQAGDNAGLL LRGTKREDVE RGQVVVKPGS ITPHTEFEAQ VYILGKDEGG RHTPFFNNYR PQFFFRTTDV TGVVNLPEGT EMVMPGDTTE MTVQLIQPIA IEEGLRFAIR EGGRTVGAGS VTKIIK //