ID   EFTU_DINSH              Reviewed;         391 AA.
AC   A8LLG2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   04-NOV-2026, entry version 99.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            EC=3.6.5.3 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Dshi_0223;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Dshi_0274;
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Roseobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12;
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA   Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA   Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA   Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA   Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA   Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT   a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
CC   -!- FUNCTION: GTP hydrolase that promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00118};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={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; CP000830; ABV91972.1; -; Genomic_DNA.
DR   EMBL; CP000830; ABV92023.1; -; Genomic_DNA.
DR   RefSeq; WP_012176905.1; NC_009952.1.
DR   SMR; A8LLG2; -.
DR   STRING; 398580.Dshi_0223; -.
DR   KEGG; dsh:Dshi_0223; -.
DR   KEGG; dsh:Dshi_0274; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_1_5; -.
DR   OMA; AACIEYQ; -.
DR   OrthoDB; 9803139at2; -.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   FunFam; 2.40.30.10:FF:000001; Elongation factor Tu; 1.
DR   FunFam; 3.40.50.300:FF:000003; Elongation factor Tu; 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; IPR050055; EF-Tu_GTPase.
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.
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   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   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; NF000766; PRK00049.1; 1.
DR   NCBIfam; NF009372; PRK12735.1; 1.
DR   NCBIfam; NF009373; PRK12736.1; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
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:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   Proteomes; UP000006833; Chromosome.
DR   AlphaFoldDB; A8LLG2; -.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..391
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000337373"
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         26
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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;  42777 MW;  B701ECE5949571A1 CRC64;
     MAKEKFERSK PHVNIGTIGH VDHGKTTLTA AITKQFGDFK AYDEIDGAPE EKARGITIST
     AHVEYETDAR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VNAADGPMPQ TREHILLGRQ
     VGIPYMVVFM NKVDQVDDEE LLELVEMEIR ELLSSYEYPG DDIPIIAGSA LAALEGRDPE
     IGEQKIAELM KAVDDYIPTP ARAVDQPFLM PIEDVFSISG RGTVVTGRVE RGVINVGDEI
     EIVGIRDTKK TTCTGVEMFR KLLDRGEAGD NIGALLRGVD REGVERGQVL CKPGSVTPHT
     KFEAEAYILT KEEGGRHTPF FANYRPQFYF RTTDVTGTVT LPEGTEMVMP GDNLKFGVEL
     IAPIAMEDGL RFAIREGGRT VGAGVVSKII E
//