ID   EFTU_BIFA0              Reviewed;         399 AA.
AC   B8DTV7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=BLA_1148;
OS   Bifidobacterium animalis subsp. lactis (strain AD011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=442563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD011;
RX   PubMed=19011029; DOI=10.1128/jb.01515-08;
RA   Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA   Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT   "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT   lactis AD011.";
RL   J. Bacteriol. 191:678-679(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:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
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DR   EMBL; CP001213; ACL29436.1; -; Genomic_DNA.
DR   RefSeq; WP_012619946.1; NC_011835.1.
DR   AlphaFoldDB; B8DTV7; -.
DR   SMR; B8DTV7; -.
DR   STRING; 442563.BLA_1148; -.
DR   KEGG; bla:BLA_1148; -.
DR   PATRIC; fig|442563.4.peg.1205; -.
DR   HOGENOM; CLU_007265_0_1_11; -.
DR   Proteomes; UP000002456; 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; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..399
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_1000201387"
FT   DOMAIN          10..209
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          62..66
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          83..86
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          138..141
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          175..177
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         83..87
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   399 AA;  44070 MW;  57F7BA8552E1B085 CRC64;
     MAKEKYERTK PHVNIGTIGH VDHGKTTLTA AISKVLHDEY PDLNPEYDFN QIDAAPEEQQ
     RGITINIAHI EYQTAKRHYA HVDCPGHADF VKNMITGAAQ MDGAILVVAA TDGPMAQTRE
     HVLLAPQVGV PKILVALNKC DMVDDEELIE LVEEEVRDLL DENGFDRDCP VVHTSAYGAL
     HDDAPDHDKW VATIKELMDD VDEYIPTPVH DLDKPFLMPI EDVFTISGRG TVVTGRVERG
     KLPINTNVEI VGIRPTQTTT FTSIETFHKQ MDECEAGDNT GLLLRGINRT DVERGQVVAA
     PGSVTPHTKF EGEVYVLTKD EGGRHSPFFS NYRPQFYFRT TDVTGVITLP EGVEMVQPGD
     HATFTVELIQ PIAMEEGLTF AVREGGHTVG SGRVTKILA
//