ID A0A0M9DBZ9_9LACO Unreviewed; 395 AA.
AC A0A0M9DBZ9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:KOY76361.1};
GN Synonyms=tufB {ECO:0000313|EMBL:GAT90110.1};
GN ORFNames=FF306_00204 {ECO:0000313|EMBL:GAT90110.1}, RZ71_08120
GN {ECO:0000313|EMBL:KOY76361.1}, RZ72_13410
GN {ECO:0000313|EMBL:KOY79180.1}, RZ78_13300
GN {ECO:0000313|EMBL:KPN82217.1};
OS Apilactobacillus kunkeei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Apilactobacillus.
OX NCBI_TaxID=148814 {ECO:0000313|EMBL:KOY76361.1, ECO:0000313|Proteomes:UP000037778};
RN [1] {ECO:0000313|Proteomes:UP000037749, ECO:0000313|Proteomes:UP000037778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAko {ECO:0000313|EMBL:KOY76361.1,
RC ECO:0000313|Proteomes:UP000037778}, LAla {ECO:0000313|EMBL:KOY79180.1,
RC ECO:0000313|Proteomes:UP000037749}, and LMbo
RC {ECO:0000313|EMBL:KPN82217.1, ECO:0000313|Proteomes:UP000050269};
RX PubMed=25953738; DOI=10.1093/gbe/evv079;
RA Tamarit D., Ellegaard K.M., Wikander J., Olofsson T., Vasquez A.,
RA Andersson S.G.;
RT "Functionally Structured Genomes in Lactobacillus kunkeei Colonizing the
RT Honey Crop and Food Products of Honeybees and Stingless Bees.";
RL Genome Biol. Evol. 7:1455-1473(2015).
RN [2] {ECO:0000313|EMBL:GAT90110.1, ECO:0000313|Proteomes:UP000186588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF30-6 {ECO:0000313|EMBL:GAT90110.1,
RC ECO:0000313|Proteomes:UP000186588};
RX PubMed=27776911; DOI=10.1016/j.syapm.2016.09.006;
RA Maeno S., Tanizawa Y., Kanesaki Y., Kubota E., Kumar H., Dicks L.,
RA Salminen S., Nakagawa J., Arita M., Endo A.;
RT "Genomic characterization of a fructophilic bee symbiont Lactobacillus
RT kunkeei reveals its niche-specific adaptation.";
RL Syst. Appl. Microbiol. 39:516-526(2016).
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:KOY76361.1}.
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DR EMBL; BDDX01000001; GAT90110.1; -; Genomic_DNA.
DR EMBL; JXCY01000006; KOY76361.1; -; Genomic_DNA.
DR EMBL; JXCZ01000019; KOY79180.1; -; Genomic_DNA.
DR EMBL; JXDF01000017; KPN82217.1; -; Genomic_DNA.
DR RefSeq; WP_053791852.1; NZ_VBSE01000043.1.
DR AlphaFoldDB; A0A0M9DBZ9; -.
DR PATRIC; fig|148814.13.peg.862; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000037749; Unassembled WGS sequence.
DR Proteomes; UP000037778; Unassembled WGS sequence.
DR Proteomes; UP000050269; Unassembled WGS sequence.
DR Proteomes; UP000186588; 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:UP000037778}.
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; 43430 MW; DD90AF8F51559670 CRC64;
MAKEHYERTK PHVNIGTIGH IDHGKTTLTA AITKVLSEKG LADASDYAQI DAAPEERERG
ITINTAHVEY STEKRHYAHI DAPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLARQVGVEY IVVFLNKTDL VDDDELVDLV EMEVRELLSE YDYPGDDIPV VRGSALKALQ
DDQEQKDVIL HLMDVVDEYI PTPERDASKP LLMPVEDVFT ITGRGTVASG RIDRGVVKIG
DEVEIIGLVE DILKTTVTGL EMFRKTLDEG EAGDNVGMLL RGVNREQVVR GQVIAAPGSI
KTHTEFKAQV YALSKEEGGR HTPFFSNYRP QFYFHTTDVT GVIELEDGVE MVMPGDNVEF
NVKLTKPVAI EKGTKFTVRE GGHTVGAGVV SDIEE
//
