ID A0A0F5JSI3_9BURK Unreviewed; 384 AA.
AC A0A0F5JSI3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN ECO:0000313|EMBL:KKB60801.1};
GN ORFNames=WM40_27110 {ECO:0000313|EMBL:KKB60801.1};
OS Robbsia andropogonis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Robbsia.
OX NCBI_TaxID=28092 {ECO:0000313|EMBL:KKB60801.1, ECO:0000313|Proteomes:UP000033618};
RN [1] {ECO:0000313|EMBL:KKB60801.1, ECO:0000313|Proteomes:UP000033618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP2807 {ECO:0000313|EMBL:KKB60801.1,
RC ECO:0000313|Proteomes:UP000033618};
RA Lopes-Santos L., Castro D.B., Ottoboni L.M., Park D., Weirc B.S.,
RA Destefano S.A.;
RT "Draft Genome Sequence of Burkholderia andropogonis type strain ICMP2807,
RT isolated from Sorghum bicolor.";
RL Submitted (MAR-2015) 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|HAMAP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKB60801.1}.
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DR EMBL; LAQU01000198; KKB60801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F5JSI3; -.
DR STRING; 28092.WM40_27110; -.
DR PATRIC; fig|28092.6.peg.6425; -.
DR Proteomes; UP000033618; Unassembled WGS sequence.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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|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}; Hydrolase {ECO:0000313|EMBL:KKB60801.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000033618}.
FT DOMAIN 1..194
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 7..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 384 AA; 41400 MW; 55839F04CE609D51 CRC64;
MNVGTIGHVD HGKTTLTAAI ATVLSKKFGG EAKAYDQIDA APEEKARGIT INTAHVEYET
ANRHYAHVDC PGHADYVKNM ITGAAQMDGA ILVCSAADGP MPQTREHILL SRQVGVPYII
VFLNKADMVD DAELLELVEM EVRELLSKYD FPGDDTPIIK GSAKLALEGD AGELGEVAIM
ALAEALDTYI PTPERAVDGT FLMPVEDVFS ISGRGTVVTG RVERGIIKVG EEVEIVGLRD
TQKTTVTGVE MFRKLLDQGQ AGDNVGVLVR GTKREDVQRG QVLAKPGSIK PHTDFTAEVY
VLSKDEGGRH TPFFNNYRPQ FYFRTTDVTG SISLPEGKEM VMPGDNVSIS VKLIAPIAME
EGLRFAIREG GRTVGAGVVA TITK
//
