EFTU_GEMAT
ID EFTU_GEMAT Reviewed; 400 AA.
AC C1A6Q3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=GAU_0871;
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC Gemmatimonas.
OX NCBI_TaxID=379066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505;
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) 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. {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; AP009153; BAH37913.1; -; Genomic_DNA.
DR RefSeq; WP_012682360.1; NC_012489.1.
DR AlphaFoldDB; C1A6Q3; -.
DR SMR; C1A6Q3; -.
DR STRING; 379066.GAU_0871; -.
DR PRIDE; C1A6Q3; -.
DR EnsemblBacteria; BAH37913; BAH37913; GAU_0871.
DR KEGG; gau:GAU_0871; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_0; -.
DR OMA; EGDKEWG; -.
DR OrthoDB; 621774at2; -.
DR Proteomes; UP000002209; 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; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
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; 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..400
FT /note="Elongation factor Tu"
FT /id="PRO_1000203011"
FT DOMAIN 10..210
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 66..70
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 87..90
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 142..145
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 180..182
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 87..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 400 AA; 44214 MW; DC0C06683B6C9097 CRC64;
MGKAKFERNK PHVNVGTIGH VDHGKTTTTA ALTKISADKG YGTKYIAYDE VAKASESQGR
RDSTKILTIA TSHVEYETEN RHYAHVDCPG HADYVKNMIT GAAQMDGAIL VVSAVDGPMP
QTREHILLAR QVNVPSVVVF LNKCDLVEDE ELLDLVELEV RELLSKYNYP GDDAPVIRGS
AINAINGDPK WVAEFMKLYE ALDSYIPEPV REVDKPFLLP VEDVFSITGR GTVATGRIER
GIVKVGEEVQ LVGYNAEKKT IVTGVEMFRK LLDEGQAGDN VGLLLRGVDK KDIERGMVLA
KPNSIKPHTK FHSEVYVLTK EEGGRHTPFF KGYRPQFYFR TTDVTGTIEL PEGMEMVMPG
DNVQMTIELI IPIAMEEQLR FAIREGGRTV GAGVVTKILA