ID E8R5G9_ISOPI Unreviewed; 406 AA. AC E8R5G9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-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 OrderedLocusNames=Isop_0113 {ECO:0000313|EMBL:ADV60710.1}; OS Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B). OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae; OC Isosphaera. OX NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV60710.1, ECO:0000313|Proteomes:UP000008631}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43644; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., Brettin T., RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.; RT "The complete sequence of chromosome of Isophaera pallida ATCC 43644."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADV60710.1, ECO:0000313|Proteomes:UP000008631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43644 / DSM 9630 / IS1B RC {ECO:0000313|Proteomes:UP000008631}; RX PubMed=21475588; DOI=10.4056/sigs.1533840; RG US DOE Joint Genome Institute (JGI-PGF); RA Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Isosphaera pallida type strain (IS1B)."; RL Stand. Genomic Sci. 4:63-71(2011). 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; CP002353; ADV60710.1; -; Genomic_DNA. DR RefSeq; WP_013562999.1; NC_014962.1. DR AlphaFoldDB; E8R5G9; -. DR STRING; 575540.Isop_0113; -. DR KEGG; ipa:Isop_0113; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_0; -. DR InParanoid; E8R5G9; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000008631; 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; 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; 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:UP000008631}. FT DOMAIN 10..211 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 86..90 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 141..144 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 406 AA; 44520 MW; DB34DB345FCB094E CRC64; MAKETFQRTK PHVNVGTIGH IDHGKTTLTA ALLKVLANQP WAGQTKVKDY AEIAKGGTVR DATKTVTIAV SHVEYESEKR HYAHIDCPGH ADYIKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ VGVPALVVFL NKIDLVDDEE LLELVEMEIR ELLSKYKFPG DEIPIIRGCA RPAYDDPTNP EKAKSILDLV KAMDEYIPDP VRDKDKPFLM PVEDVFSIKG RGTVGTGKVE RGVVKVGDPV EIIGFGANLK STVTGVEMFQ KVLEQGEAGD NVGVLLRGIE KNQLERGQVI CKPGSITPHT KFEAEVYVLS KDEGGRHTPF FKNYRPQFYF RTTDVTGTVL NLLAEDGSEA QMCMPGDNIK MTVELQTPIA MEENLRFAIR EGGRTVGAGV VTKILA //