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EFTU_VIBC3
ID   EFTU_VIBC3              Reviewed;         394 AA.
AC   A5F3K0; C3M3X9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA;
GN   OrderedLocusNames=VC0395_A2723, VC395_0364;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufB;
GN   OrderedLocusNames=VC0395_A2774, VC395_0405;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ21011.1; -; Genomic_DNA.
DR   EMBL; CP000627; ABQ21384.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08387.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08428.1; -; Genomic_DNA.
DR   RefSeq; WP_000031644.1; NZ_CP045719.1.
DR   AlphaFoldDB; A5F3K0; -.
DR   SMR; A5F3K0; -.
DR   STRING; 345073.VC395_0364; -.
DR   EnsemblBacteria; ABQ21011; ABQ21011; VC0395_A2774.
DR   EnsemblBacteria; ABQ21384; ABQ21384; VC0395_A2723.
DR   GeneID; 57739099; -.
DR   KEGG; vco:VC0395_A2723; -.
DR   KEGG; vco:VC0395_A2774; -.
DR   KEGG; vcr:VC395_0364; -.
DR   KEGG; vcr:VC395_0405; -.
DR   PATRIC; fig|345073.21.peg.352; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_0_6; -.
DR   OMA; EGDKEWG; -.
DR   Proteomes; UP000000249; Chromosome 2.
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..394
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000337567"
FT   DOMAIN          10..204
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   394 AA;  43126 MW;  BF0DE31A00618B36 CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AICTVLAKVY GGKARDFASI DNAPEERERG
     ITINTSHVEY DTPNRHYAHV DCPGHADYVK NMITGAAQMD GGILVVAATD GPMPQTREHI
     LLGRQVGIPY IIVFMNKCDM VDDEELLELV EMEVRELLSE YDFPGDDLPV IQGSALGALN
     GEAQWEAKIV ELAEALDTYI PEPERAVDMA FLMPIEDVFS IQGRGTVVTG RIERGILKVG
     DEVAIVGIKE TVKTTCTGVE MFRKLLDEGR AGENVGALLR GTKREEVERG QVLAKPGSIT
     PHTKFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG SIELPEGVEM VMPGDNVKMV
     VDLIAPIAMD EGLRFAIREG GRTVGAGVVA KIIA
 
 
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