ID   EFTU_CERS5              Reviewed;         391 AA.
AC   A4WVL0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Rsph17025_2536;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Rsph17025_2549;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000661; ABP71424.1; -; Genomic_DNA.
DR   EMBL; CP000661; ABP71437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WVL0; -.
DR   SMR; A4WVL0; -.
DR   STRING; 349102.Rsph17025_2536; -.
DR   EnsemblBacteria; ABP71424; ABP71424; Rsph17025_2536.
DR   EnsemblBacteria; ABP71437; ABP71437; Rsph17025_2549.
DR   KEGG; rsq:Rsph17025_2536; -.
DR   KEGG; rsq:Rsph17025_2549; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_1_5; -.
DR   OMA; EGDKEWG; -.
DR   OrthoDB; 621774at2; -.
DR   BioCyc; RSPH349102:G1G8M-2614-MON; -.
DR   BioCyc; RSPH349102:G1G8M-2628-MON; -.
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   Gene3D; 3.40.50.300; -; 1.
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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 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.
FT   CHAIN           1..391
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000337490"
FT   DOMAIN          10..201
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          55..59
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          76..79
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          131..134
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          169..171
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         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         131..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   391 AA;  42875 MW;  1163373768E7DE42 CRC64;
     MAKAKFERNK PHVNIGTIGH VDHGKTTLTA AITKYFGEFR AYDQIDGAPE ERARGITIST
     AHVEYESESR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VNAADGPMPQ TREHILLGRQ
     VGIPYMVVYM NKVDQVDDPE LLELVEMEIR ELLSSYDYPG DDIPIIKGSA LAAMNGTDKE
     IGEDSIRALI AAVDEYIPTP ARAVDQPFLM PVEDVFSISG RGTVATGRIE RGVVKVGEEL
     EIVGIRPSKK TVCTGVEMFR KLLDQGEAGD NVGLLLRGVD RDGIERGQVL CKPGSVKPHT
     KFEAEAYILT KEEGGRHTPF FANYRPQFYF RTTDVTGTVE LPEGTEMVMP GDNLKFNVEL
     IAPIAMEEKL RFAIREGGRT VGAGVVSKII A