ID W0GW14_9SYNE Unreviewed; 399 AA.
AC W0GW14;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=tufA {ECO:0000313|EMBL:AHF62734.1};
GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN ORFNames=Syncc8109_0325 {ECO:0000313|EMBL:AHF62734.1};
OS Synechococcus sp. WH 8109.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=166314 {ECO:0000313|EMBL:AHF62734.1, ECO:0000313|Proteomes:UP000002780};
RN [1] {ECO:0000313|EMBL:AHF62734.1, ECO:0000313|Proteomes:UP000002780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8109 {ECO:0000313|EMBL:AHF62734.1,
RC ECO:0000313|Proteomes:UP000002780};
RA Sabehi G., Feingersch R., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.H., Freidman R., Frazier M., Venter J.C., Lindell D.;
RL Submitted (MAY-2012) 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:0000256|HAMAP-Rule:MF_00118}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC 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; CP006882; AHF62734.1; -; Genomic_DNA.
DR RefSeq; WP_006851621.1; NZ_CP006882.1.
DR AlphaFoldDB; W0GW14; -.
DR SMR; W0GW14; -.
DR STRING; 166314.Syncc8109_0325; -.
DR KEGG; syh:Syncc8109_0325; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_3; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000002780; 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 {ECO:0000256|ARBA:ARBA00022490, 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};
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}.
FT DOMAIN 10..204
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 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 399 AA; 43590 MW; 020E83FC4A96AD92 CRC64;
MAREKFERNK PHVNIGTIGH VDHGKTTLTA AITNVLAKKG QAEVQNYADI DGAPEERERG
ITINTAHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GAILVCAATD GPMAQTKEHI
LLAKQVGVPA LVVALNKCDM VDDEEIIELV EMEIRELLSS YDFPGDDIPV VQVSGLKAIE
GEAEWEAKIE ELMAAVDSSI PEPEREVDKP FLMAVEDVFS ITGRGTVATG RIERGIVKVG
EEIEIVGIKD TRKTTVTGVE MFRKLLDEGM AGDNVGLLLR GIQKEDIERG MVLVKPGSIT
PHTKFEGQVY VLKKEEGGRH TPFFAGYRPQ FYIRTTDVTG QITAFTAEDG SNVEMVMPGD
NIQMTGELIC PVAIEQGMRF AIREGGRTIG AGVVSKIIE
//
