ID   D8ICZ6_BRAP9            Unreviewed;       408 AA.
AC   D8ICZ6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=BP951000_1028 {ECO:0000313|EMBL:ADK31019.1};
OS   Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK31019.1, ECO:0000313|Proteomes:UP000000332};
RN   [1] {ECO:0000313|EMBL:ADK31019.1, ECO:0000313|Proteomes:UP000000332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX   PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA   Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA   Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT   "The complete genome sequence of the pathogenic intestinal spirochete
RT   Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL   PLoS ONE 5:E11455-E11455(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}.
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DR   EMBL; CP002025; ADK31019.1; -; Genomic_DNA.
DR   RefSeq; WP_013243972.1; NC_014330.1.
DR   AlphaFoldDB; D8ICZ6; -.
DR   STRING; 759914.BP951000_1028; -.
DR   GeneID; 56439593; -.
DR   KEGG; bpo:BP951000_1028; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_1_12; -.
DR   InParanoid; D8ICZ6; -.
DR   Proteomes; UP000000332; 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:UP000000332}.
FT   DOMAIN          10..219
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         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         143..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   408 AA;  44512 MW;  D615C1A8D89D08FF CRC64;
     MAKGTYEGTK THVNVGTIGH VDHGKTTLTS AITAVSSAMF PATVQKVAYD SVAKASESQG
     RRDPTKILTI ATSHVEYESD NRHYAHVDCP GHADYIKNMI TGAAQMDGAI LVVSAEDGVM
     PQTKEHVLLS RQVGVNYIVV FLNKCDKLDD PEMAEIVEAE VVDVLDHYGF DGSKTPIIRG
     SAIKAIQAIE AGKDPRTDPD CKCILDLLNA LDTYIPDPVR ETDKDFLMSI EDVYSIPGRG
     TVVTGRIERG QIKKGDEVEI VGLRETKKTT CTGVEMFKKE VVGIAGYNVG CLLRGIERKE
     VERGQVLAKP GTITPHKKFE AEVYILKKEE GGRHSGFVSG YRPQMYFRTT DVTGVINLPE
     GSPMIMPGDN ANLTIELISQ IAMEEKQRFA IREGGKTVGN GVVTKILE
//