ID   EFTU_SYNJB              Reviewed;         409 AA.
AC   Q2JMX7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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}; OrderedLocusNames=CYB_0921;
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13);
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000240; ABD01900.1; -; Genomic_DNA.
DR   RefSeq; WP_011432556.1; NC_007776.1.
DR   AlphaFoldDB; Q2JMX7; -.
DR   SMR; Q2JMX7; -.
DR   STRING; 321332.CYB_0921; -.
DR   KEGG; cyb:CYB_0921; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_0_3; -.
DR   OMA; EGDKEWG; -.
DR   OrthoDB; 621774at2; -.
DR   Proteomes; UP000001938; 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   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; Reference proteome.
FT   CHAIN           1..409
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_1000015769"
FT   DOMAIN          10..214
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
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         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   409 AA;  44855 MW;  769DB694C9A4542D CRC64;
     MARAKFERTK PHVNVGTIGH VDHGKTTLTA AITTTLAALG QATAKRYDEI DAAPEEKARG
     ITINTAHVEY QTANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPS LVVFLNKADM VDDPELLELV ELEVRELLSK YDFPGDDVPI IRGSALKALE
     RMTANPKTQR GEDPWVDKIY ELMDAVDSYI PTPERDVDKP FLMAVEDVFS ITGRGTVATG
     RIERGRIKVG ETVELVGLRE TRSTTVTGLE MFQKTLDEGI AGDNVGVLLR GIQKNEVERG
     MVLAKPKTIT PHTNFESEVY VLKKEEGGRH TPFFAGYRPQ FYVRTTDVTG TISSFTADDG
     SQPEMVMPGD RVKMTVELIQ PIAIEQGMRF AIREGGRTVG AGVVSKILK