ID   F7XW13_MIDMI            Unreviewed;       392 AA.
AC   F7XW13;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, 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=tufB {ECO:0000313|EMBL:AEI88862.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=midi_00560 {ECO:0000313|EMBL:AEI88862.1};
OS   Midichloria mitochondrii (strain IricVA).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Candidatus Midichloriaceae; Midichloria.
OX   NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88862.1, ECO:0000313|Proteomes:UP000006639};
RN   [1] {ECO:0000313|EMBL:AEI88862.1, ECO:0000313|Proteomes:UP000006639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IricVA {ECO:0000313|EMBL:AEI88862.1,
RC   ECO:0000313|Proteomes:UP000006639};
RX   PubMed=21690562; DOI=10.1093/molbev/msr159;
RA   Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
RA   Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
RA   Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
RT   "Phylogenomic evidence for the presence of a flagellum and cbb3 oxidase in
RT   the free-living mitochondrial ancestor.";
RL   Mol. Biol. Evol. 28:3285-3296(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}.
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DR   EMBL; CP002130; AEI88862.1; -; Genomic_DNA.
DR   RefSeq; WP_013951074.1; NC_015722.1.
DR   AlphaFoldDB; F7XW13; -.
DR   STRING; 696127.midi_00560; -.
DR   KEGG; mmn:midi_00560; -.
DR   HOGENOM; CLU_007265_0_1_5; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000006639; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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}; Hydrolase {ECO:0000313|EMBL:AEI88862.1};
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:UP000006639}.
FT   DOMAIN          10..201
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         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         131..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   392 AA;  43088 MW;  ADCED9395F4EC06F CRC64;
     MAKEKFVRNK PHVNIGTIGH VDHGKTSLTA ALTKMFGRYV KYDEIDKAPE EKARGITINS
     AHVEYETENR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ
     VGVPALVVFL NKVDMVDDPE LLELVEMEVR DLLNQYGFPG DQIPVIKGSA LMALEGKNPA
     LGEEAIKELM KQVDEYIPLP TRSVDKPFLM PVEDVFSISG RGTVATGRVE QGVVKVGEEI
     EIVGLKAQSS KTTCTGVEMF RRLLDQGEAG DNVGLLLRGI ERDQIERGQV LAKPGTIKPH
     KKFRAEVYIL KKEEGGRHTP FVSNYRPQFY FRTTDVTGTI NLKAGVEMVM PGDNTEIMVE
     LISPIAMDKG LKFAIREGGR TVGAGVVAEI IE
//