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EFTU_LACP3
ID   EFTU_LACP3              Reviewed;         396 AA.
AC   Q039K9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=LSEI_1332;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC   B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000423; ABJ70113.1; -; Genomic_DNA.
DR   RefSeq; WP_003565275.1; NC_008526.1.
DR   RefSeq; YP_806555.1; NC_008526.1.
DR   AlphaFoldDB; Q039K9; -.
DR   SMR; Q039K9; -.
DR   STRING; 321967.LSEI_1332; -.
DR   EnsemblBacteria; ABJ70113; ABJ70113; LSEI_1332.
DR   GeneID; 61269552; -.
DR   KEGG; lca:LSEI_1332; -.
DR   PATRIC; fig|321967.11.peg.1311; -.
DR   HOGENOM; CLU_007265_0_1_9; -.
DR   OMA; ERPHCNV; -.
DR   Proteomes; UP000001651; Chromosome.
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   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.
FT   CHAIN           1..396
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000337413"
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;  43573 MW;  9EA44A90F7DDAB26 CRC64;
     MAEKEHYERT KPHVNIGTIG HVDHGKTTLT AAITKVLSEK GLAKAQDYAS IDAAPEEKER
     GITINTAHVE YETEKRHYAH IDAPGHADYV KNMITGAAQM DGAILVVAAT DGPMPQTREH
     ILLARQVGVD YIVVFLNKTD LVDDPELIDL VEMEVRELLS EYDYPGDDIP VIRGSALKAL
     EGDPEQEKVI MELMDTIDEY IPTPVRETDK PFLMPVEDVF TITGRGTVAS GRIDRGTVKI
     GDEVEIIGLK PDVIKSTVTG LEMFRKTLDL GEAGDNVGVL LRGVNREQVE RGQVLAKPGS
     IQLHNKFKGE VYILTKEEGG RHTPFFSNYR PQFYFHTTDV TGVIELPDGV EMVMPGDNVT
     FEVDLIAPVA IEKGTKFTVR EGGRTVGAGV VSEILD
 
 
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