EFTU_STIAU
ID EFTU_STIAU Reviewed; 396 AA.
AC P42479; Q53775;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 104.
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}; Synonyms=tufB;
OS Stigmatella aurantiaca.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Archangiaceae; Stigmatella.
OX NCBI_TaxID=41;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DW4;
RX PubMed=7784178; DOI=10.1093/nar/23.10.1737;
RA Bremaud L., Fremaux C., Laalami S., Cenatiempo Y.;
RT "Genetic and molecular analysis of the tRNA-tufB operon of the
RT myxobacterium Stigmatella aurantiaca.";
RL Nucleic Acids Res. 23:1737-1743(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-396.
RC STRAIN=SGA1;
RX PubMed=8085791; DOI=10.1007/bf00873088;
RA Ludwig W., Neumaier J., Klugbauer N., Brockmann E., Roller C.,
RA Klugbauer S., Reetz K., Schachtner I., Ludvigsen A., Bachleitner M.,
RA Fischer U., Schleifer K.H.;
RT "Phylogenetic relationships of Bacteria based on comparative sequence
RT analysis of elongation factor Tu and ATP-synthase beta-subunit genes.";
RL Antonie Van Leeuwenhoek 64:285-305(1993).
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; X82820; CAA58029.1; -; Genomic_DNA.
DR EMBL; X76870; CAA54197.1; -; Genomic_DNA.
DR PIR; S55281; S55281.
DR AlphaFoldDB; P42479; -.
DR SMR; P42479; -.
DR PRIDE; P42479; -.
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.
FT CHAIN 1..396
FT /note="Elongation factor Tu"
FT /id="PRO_0000091398"
FT DOMAIN 10..206
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 286
FT /note="R -> P (in Ref. 2; CAA54197)"
FT /evidence="ECO:0000305"
FT CONFLICT 297..298
FT /note="NW -> KP (in Ref. 2; CAA54197)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="E -> D (in Ref. 2; CAA54197)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="P -> R (in Ref. 2; CAA54197)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="V -> L (in Ref. 2; CAA54197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43367 MW; B091C0A6AA7FF721 CRC64;
MAKEKFERNK PHVNIGTIGH VDHGKTSLTA AITKVLAKTG GATFLAYDQI DKAPEERERG
ITISTAHVEY QTKNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
LLARQVGVPY IVVFLNKVDM LDDPELRELV EMEVRDLLKK YEFPGDSIPI IPGSALKALE
GDTSDIGEGA ILKLMAAVDE YIPTPQRATD KPFLMPVEDV FSIAGRGTVA TGRVERGKIK
VGEEVEIVGI RPTQKTVITG VEMFRKLLDE GMAGDNIGAL LRGLKREDLE RGQVLANWGS
INPHTKFKAQ VYVLSKEEGG RHTPFFKGYR PQFYFRTTDV TGTVKLPDNV EMVMPGDNIA
IEVELITPVA MEKELPFAIR EGGRTVGAGV VADIIA
