ID A0A192H546_9LACO Unreviewed; 395 AA.
AC A0A192H546;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:ANK63096.1};
GN ORFNames=AYR53_10185 {ECO:0000313|EMBL:ANK63096.1}, OUQ91_002249
GN {ECO:0000313|EMBL:MDA5387100.1};
OS Loigolactobacillus backii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=375175 {ECO:0000313|EMBL:ANK63096.1, ECO:0000313|Proteomes:UP000078582};
RN [1] {ECO:0000313|EMBL:ANK63096.1, ECO:0000313|Proteomes:UP000078582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMW 1.1989 {ECO:0000313|EMBL:ANK63096.1,
RC ECO:0000313|Proteomes:UP000078582};
RA Behr J., Geissler A.J., Vogel R.F.;
RT "Pediococcus and Lactobacillus from brewery environment - whole genome
RT sequencing and assembly.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MDA5387100.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KKP 3565 {ECO:0000313|EMBL:MDA5387100.1};
RG Lg backii sequencing group;
RA Kiousi D.E., Bucka Kolendo J.;
RL Submitted (NOV-2022) 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; CP014873; ANK63096.1; -; Genomic_DNA.
DR EMBL; JAPTYS010000006; MDA5387100.1; -; Genomic_DNA.
DR RefSeq; WP_068224739.1; NZ_RHNQ01000004.1.
DR STRING; 375175.AYR53_10185; -.
DR GeneID; 42982625; -.
DR KEGG; lbt:AYR52_05165; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000078582; Chromosome.
DR Proteomes; UP001150357; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000078582}.
FT DOMAIN 10..204
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 395 AA; 43499 MW; 198D759BB39E5FB7 CRC64;
MAKEHYERTK PHVNIGTIGH IDHGKTTLTA AITKVLAAKG LAKAEDYATI DSAPEERERG
ITINTAHVEY ETEKRHYAHI DAPGHADYIK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLARQVGVEY IVVFLNKTDL VDDPELTDLV EMETRELLSE YDYPGDDIPF IRGSALKALE
GDKDEEAHIM ELLDAVDDYI PTPERNNELP FLMPVEDVFT ITGRGTVASG RIDRGMVKVG
DEVEILGLEP EVLKSTVTGL EMFRKTLDYG EAGDNVGVLL RGVNREQVVR GQVLAKPGSI
KVHDKFKGQA YILSKEEGGR HTPFFSNYRP QFYFHTTDVT GVITLPENVE MVMPGDNVEF
SVDLIAPVAV EKGTKFTVRE GGRTVGAGVV TEIDE
//
