ID   Q5E228_ALIF1            Unreviewed;       394 AA.
AC   Q5E228;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 139.
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=tufA {ECO:0000313|EMBL:AAW86918.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufB
GN   {ECO:0000313|EMBL:AAW84728.1};
GN   OrderedLocusNames=VF_0233 {ECO:0000313|EMBL:AAW84728.1}, VF_2423
GN   {ECO:0000313|EMBL:AAW86918.1};
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW86918.1, ECO:0000313|Proteomes:UP000000537};
RN   [1] {ECO:0000313|EMBL:AAW86918.1, ECO:0000313|Proteomes:UP000000537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537}, and
RC   ES114 {ECO:0000313|EMBL:AAW86918.1};
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
RN   [2] {ECO:0000313|EMBL:AAW86918.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ES114 {ECO:0000313|EMBL:AAW86918.1};
RX   PubMed=18366731; DOI=10.1186/1471-2164-9-138;
RA   Mandel M.J., Stabb E.V., Ruby E.G.;
RT   "Comparative genomics-based investigation of resequencing targets in Vibrio
RT   fischeri: focus on point miscalls and artefactual expansions.";
RL   BMC Genomics 9:138-138(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: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; CP000020; AAW84728.1; -; Genomic_DNA.
DR   EMBL; CP000020; AAW86918.1; -; Genomic_DNA.
DR   RefSeq; WP_005417220.1; NC_006840.2.
DR   RefSeq; YP_203616.1; NC_006840.2.
DR   RefSeq; YP_205806.1; NC_006840.2.
DR   AlphaFoldDB; Q5E228; -.
DR   STRING; 312309.VF_0233; -.
DR   EnsemblBacteria; AAW84728; AAW84728; VF_0233.
DR   EnsemblBacteria; AAW86918; AAW86918; VF_2423.
DR   GeneID; 77253669; -.
DR   KEGG; vfi:VF_0233; -.
DR   KEGG; vfi:VF_2423; -.
DR   PATRIC; fig|312309.11.peg.230; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_0_6; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000000537; Chromosome I.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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:UP000000537}.
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   394 AA;  43208 MW;  93EE8BE57C7775D7 CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AICTTLAKIY GGVAKDFASI DNAPEERERG
     ITISTSHVEY DTPARHYAHV DCPGHADYVK NMITGAAQMD GGILVVAATD GPMPQTREHI
     LLGRQVGIPY IIVFMNKCDM VDDEELLELV EMEVRELLSE YDFPGDDLPV IQGSALGALN
     GEKEWEDKIV ELAEALDSYI PEPERAVDQP FLLPIEDVFS IQGRGTVVTG RIERGILRVG
     DEVEIVGIKE TTMTTCTGVE MFRKLLDEGR AGENVGALLR GTKRDDVERG QVLAAKGSIN
     PHTKFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG DITLPEGVEM VMPGDNVQMT
     VELIAPIAMD EGLRFAIREG GRTVGAGVVA KIFA
//