ID EFTU_SYNE7 Reviewed; 409 AA.
AC P33171; Q31PV5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 27-MAR-2024, entry version 141.
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};
GN OrderedLocusNames=Synpcc7942_0884;
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2110445; DOI=10.1007/bf00249075;
RA Ludwig W., Weizenegger M., Betzl D., Leidel E., Lenz T., Ludvigsen A.,
RA Moellenhoff D., Wenzig P., Schleifer K.H.;
RT "Complete nucleotide sequences of seven eubacterial genes coding for the
RT elongation factor Tu: functional, structural and phylogenetic
RT evaluations.";
RL Arch. Microbiol. 153:241-247(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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.
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; CP000100; ABB56914.1; -; Genomic_DNA.
DR PIR; S04430; S04430.
DR RefSeq; WP_011242968.1; NZ_JACJTX010000005.1.
DR AlphaFoldDB; P33171; -.
DR SMR; P33171; -.
DR STRING; 1140.Synpcc7942_0884; -.
DR PaxDb; 1140-Synpcc7942_0884; -.
DR GeneID; 76399632; -.
DR KEGG; syf:Synpcc7942_0884; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_3; -.
DR OrthoDB; 9804504at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0884-MONOMER; -.
DR Proteomes; UP000889800; 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; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..409
FT /note="Elongation factor Tu"
FT /id="PRO_0000091417"
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"
FT CONFLICT 325
FT /note="E -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 44190 MW; DB6F96A7F8E40D20 CRC64;
MARAKFERTK PHANIGTIGH VDHGKTTLTA AITTVLAKAG MAKARAYADI DAAPEEKARG
ITINTAHVEY ETGNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
LLAKQVGVPN IVVFLNKEDM VDDAELLELV ELEVRELLSS YDFPGDDIPI VAGSALQALE
AIQGGASGQK GDNPWVDKIL KLMEEVDAYI PTPEREVDRP FLMAVEDVFT ITGRGTVATG
RIERGSVKVG ETIEIVGLRD TRSTTVTGVE MFQKTLDEGL AGDNVGLLLR GIQKTDIERG
MVLAKPGSIT PHTKFESEVY VLKKEEGGRH TPFFPGYRPQ FYVRTTDVTG AISDFTADDG
SAAEMVIPGD RIKMTVELIN PIAIEQGMRF AIREGGRTIG AGVVSKILQ
//
