ID   C7NCD6_LEPBD            Unreviewed;       394 AA.
AC   C7NCD6;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=Lebu_1919 {ECO:0000313|EMBL:ACV39782.1};
OS   Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 /
OS   NCTC 10249 / C-1013-b).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV39782.1, ECO:0000313|Proteomes:UP000001910};
RN   [1] {ECO:0000313|EMBL:ACV39782.1, ECO:0000313|Proteomes:UP000001910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC   {ECO:0000313|Proteomes:UP000001910};
RX   PubMed=21304648; DOI=10.4056/sigs.1854;
RA   Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA   Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA   Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT   b).";
RL   Stand. Genomic Sci. 1:126-132(2009).
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}.
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DR   EMBL; CP001685; ACV39782.1; -; Genomic_DNA.
DR   RefSeq; WP_015770120.1; NC_013192.1.
DR   AlphaFoldDB; C7NCD6; -.
DR   STRING; 523794.Lebu_1919; -.
DR   KEGG; lba:Lebu_1919; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_0_0; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000001910; 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}.
FT   DOMAIN          10..204
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   394 AA;  43225 MW;  3C03D9BAC10C1486 CRC64;
     MAKAKFERSK PHVNVGTIGH VDHGKTTTTA AISKVLAEKG LAEKVDFENI DQAPEERERG
     ITINTAHIEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPY IVVYLNKVDM VDDEELLELV EMEVRELLTE YGFPGDDVPV IKGSSLGALN
     GEQKWIDAIV ELMDAVDEYI PTPERPVDQS FLMPIEDVFT ITGRGTVVTG RVERGVIKVG
     EEVEIVGIKP TTKTTVTGVE MFRKLLDSGQ AGDNIGALLR GTKKEEVERG QVLAKPGTIN
     PHTGFKSEVY VLTKDEGGRH TPFFTGYKPQ FYFRTTDITG EVNLPEGVEM VMPGDNIEMT
     VELIHPIAME EGLRFAIREG GRTVASGVVA TITK
//