EFTU3_STRCO
ID EFTU3_STRCO Reviewed; 392 AA.
AC P40175; Q9K412;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Elongation factor Tu-3 {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu-3 {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf3 {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=SCO1321;
GN ORFNames=2SCG61.03c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=7918656; DOI=10.1016/0167-4781(94)90085-x;
RA van Wezel G.P., Woudt L.P., Vervenne R., Verdurmen M.L., Vijgenboom E.,
RA Bosch L.;
RT "Cloning and sequencing of the tuf genes of Streptomyces coelicolor
RT A3(2).";
RL Biochim. Biophys. Acta 1219:543-547(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; X77040; CAA54330.1; -; Genomic_DNA.
DR EMBL; AL939108; CAB95778.1; -; Genomic_DNA.
DR PIR; S50139; S50139.
DR RefSeq; NP_625606.1; NC_003888.3.
DR RefSeq; WP_003977508.1; NZ_VNID01000006.1.
DR AlphaFoldDB; P40175; -.
DR SMR; P40175; -.
DR STRING; 100226.SCO1321; -.
DR GeneID; 1096744; -.
DR KEGG; sco:SCO1321; -.
DR PATRIC; fig|100226.15.peg.1324; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_11; -.
DR InParanoid; P40175; -.
DR OMA; TFGKPME; -.
DR PhylomeDB; P40175; -.
DR Proteomes; UP000001973; 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; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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..392
FT /note="Elongation factor Tu-3"
FT /id="PRO_0000091402"
FT DOMAIN 10..206
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 63..67
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 84..87
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 139..142
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 176..178
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 84..88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 139..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT CONFLICT 236
FT /note="R -> P (in Ref. 1; CAA54330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 41676 MW; 16E8CCC3A864B23A CRC64;
MSKTAYVRTK PHLNIGTMGH VDHGKTTLTA AITKVLAERG AGSTTQYVSF DRIDRAPEEA
ARGITINIAH VEYETDTRHY AHVDMPGHAD YVKNMVTGAA QLDGAILVVS ALDGIMPQTA
EHVLLARQVG VDHIVVALNK ADAGDEELTD LVELEVRELL TAHGYGGDAV PVVRVSGLKA
LEGDPRWTAS VEALLDAVDT YVPMPERYLD APFLLPVENV LTITGRGTVV TGAVERGTVR
VGDRVEVLGA SVETVVTGLE TFGKPMEEAQ AGDNVALLLR GVARDTVRRG QVVAAPGSVV
PARRFRARVY VLSAREGGRS TPLTTGYRPQ FYIRTADVVG DVDLGEEAVA RPGDTVTMTV
ELGRDVPLET GLGFAIREGG RTVGAGTVTA VE
