EFTU_LACJO
ID EFTU_LACJO Reviewed; 396 AA.
AC Q74JU6; Q6UE10;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=LJ_1009;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14602655; DOI=10.1128/aem.69.11.6908-6922.2003;
RA Ventura M., Canchaya C., Meylan V., Klaenhammer T.R., Zink R.;
RT "Analysis, characterization, and loci of the tuf genes in lactobacillus and
RT bifidobacterium species and their direct application for species
RT identification.";
RL Appl. Environ. Microbiol. 69:6908-6922(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AY372049; AAR25444.1; -; Genomic_DNA.
DR EMBL; AE017198; AAS08831.1; -; Genomic_DNA.
DR RefSeq; WP_004894320.1; NC_005362.1.
DR AlphaFoldDB; Q74JU6; -.
DR SMR; Q74JU6; -.
DR STRING; 257314.LJ_1009; -.
DR MoonProt; Q74JU6; -.
DR EnsemblBacteria; AAS08831; AAS08831; LJ_1009.
DR GeneID; 66435577; -.
DR KEGG; ljo:LJ_1009; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_9; -.
DR OMA; ERPHCNV; -.
DR Proteomes; UP000000581; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0010339; C:external side of cell wall; IDA:CAFA.
DR GO; GO:0009275; C:Gram-positive-bacterium-type cell wall; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
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 GO; GO:0044651; P:adhesion of symbiont to host epithelial cell; IDA:CAFA.
DR GO; GO:0044068; P:modulation by symbiont of host cellular process; IDA:CAFA.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:CAFA.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 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; PS00301; G_TR_1; 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..396
FT /note="Elongation factor Tu"
FT /id="PRO_0000337418"
FT DOMAIN 11..205
FT /note="tr-type G"
FT REGION 20..27
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 61..65
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 82..85
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 137..140
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 175..177
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 396 AA; 43664 MW; 2A42424651F5DD08 CRC64;
MAEKEHYERT KPHVNIGTIG HVDHGKTTLT AAITTVLAED GLAQAEDYSQ IDAAPEEKER
GITINTAHVE YETKNRHYAH MDAPGHADYI KNMITGAAQM DGAILVVAAT DGPMPQTREH
ILLARQVGVQ YIVVFLNKVD LVDDPELIDL VEMEVRDLLS EYDYPGDDVP VIRGSALKAL
EGDPEQQDVI RKLMETVDEY IPTPERDTDK PFLMPVEDVF TITGRGTVAS GRIDRGTVKV
GDEVEIVGLT DKIEKSTVTG LEMFHKTLDL GEAGDNVGVL LRGIDRDQVE RGQVLAAPGS
IQTHKNFKGQ VYILNKDEGG RHTPFFSDYR PQFYFHTTDV TGKIELPEGT EMVMPGDNVE
FTVELIKPVA IEKGTKFTIR EGGKTVGAGQ VTEILD
