ID A0A124SV67_9BURK Unreviewed; 396 AA.
AC A0A124SV67;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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:KVV56123.1};
GN ORFNames=BTE28158_05456 {ECO:0000313|EMBL:VWC13759.1}, BTE28158_05470
GN {ECO:0000313|EMBL:VWC14009.1}, WT27_24915
GN {ECO:0000313|EMBL:KVV56123.1}, WT27_24985
GN {ECO:0000313|EMBL:KVV56136.1}, WT83_00800
GN {ECO:0000313|EMBL:KWN05975.1}, WT83_00870
GN {ECO:0000313|EMBL:KWN05988.1};
OS Burkholderia territorii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=1503055 {ECO:0000313|EMBL:KVV56123.1, ECO:0000313|Proteomes:UP000062317};
RN [1] {ECO:0000313|Proteomes:UP000062317, ECO:0000313|Proteomes:UP000068016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB1301WGS {ECO:0000313|EMBL:KVV56123.1,
RC ECO:0000313|Proteomes:UP000062317}, and MSMB793WGS
RC {ECO:0000313|EMBL:KWN05975.1, ECO:0000313|Proteomes:UP000068016};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VWC13759.1, ECO:0000313|Proteomes:UP000494175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28158 {ECO:0000313|EMBL:VWC13759.1};
RA Depoorter E.;
RL Submitted (SEP-2019) 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}.
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DR EMBL; LPEQ01000022; KVV56123.1; -; Genomic_DNA.
DR EMBL; LPEQ01000022; KVV56136.1; -; Genomic_DNA.
DR EMBL; LPLZ01000078; KWN05975.1; -; Genomic_DNA.
DR EMBL; LPLZ01000078; KWN05988.1; -; Genomic_DNA.
DR EMBL; CABVPO010000050; VWC13759.1; -; Genomic_DNA.
DR EMBL; CABVPO010000050; VWC14009.1; -; Genomic_DNA.
DR RefSeq; WP_034209732.1; NZ_VOWZ01000024.1.
DR AlphaFoldDB; A0A124SV67; -.
DR GeneID; 46198962; -.
DR KEGG; btei:WS51_12100; -.
DR KEGG; btei:WS51_12170; -.
DR Proteomes; UP000062317; Unassembled WGS sequence.
DR Proteomes; UP000068016; Unassembled WGS sequence.
DR Proteomes; UP000494175; 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};
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}.
FT DOMAIN 10..206
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 396 AA; 43047 MW; A437A41CCCE3CAFD CRC64;
MAKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLTKKF GGEAKAYDQI DAAPEEKARG
ITINTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
LLARQVGVPY IIVFLNKCDM VDDAELLELV EMEVRELLSK YDFPGDDTPI VKGSAKLALE
GDTGELGEVA IMNLADALDT YIPTPERAVD GAFLMPVEDV FSISGRGTVV TGRVERGIIK
VGEEIEIVGI KPTVKTTCTG VEMFRKLLDQ GQAGDNVGIL LRGTKREDVE RGQVLAKPGS
ITPHTHFTAE VYVLSKDEGG RHTPFFNNYR PQFYFRTTDV TGSIELPKDK EMVMPGDNVS
ITVKLIAPIA MEEGLRFAIR EGGRTVGAGV VAKIIE
//
