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Database: UniProt
Entry: A0A0F5EWN5_AVIPA
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ID   A0A0F5EWN5_AVIPA        Unreviewed;       394 AA.
AC   A0A0F5EWN5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
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_1 {ECO:0000313|EMBL:SUU98172.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:QIR12485.1};
GN   ORFNames=HBL79_09850 {ECO:0000313|EMBL:QIR12485.1}, HBL79_11555
GN   {ECO:0000313|EMBL:QIR12786.1}, NCTC10926_01591
GN   {ECO:0000313|EMBL:SUU98172.1};
OS   Avibacterium paragallinarum (Haemophilus gallinarum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Avibacterium.
OX   NCBI_TaxID=728 {ECO:0000313|EMBL:SUU98172.1, ECO:0000313|Proteomes:UP000254620};
RN   [1] {ECO:0000313|EMBL:SUU98172.1, ECO:0000313|Proteomes:UP000254620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10926 {ECO:0000313|EMBL:SUU98172.1,
RC   ECO:0000313|Proteomes:UP000254620};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QIR12485.1, ECO:0000313|Proteomes:UP000503595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESV-135 {ECO:0000313|EMBL:QIR12485.1,
RC   ECO:0000313|Proteomes:UP000503595};
RA   Cobos-Justo M.E., Sanchez-Alonso M.P., Negrete-Abascal E., Perez V.,
RA   Soriano-Vargas E., Castelan H., Vazquez-Cruz C.;
RT   "Comparison of the genome sequence of three Mexican strains of Avibacterium
RT   paragallinarum.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; CP050316; QIR12485.1; -; Genomic_DNA.
DR   EMBL; CP050316; QIR12786.1; -; Genomic_DNA.
DR   EMBL; UFSW01000001; SUU98172.1; -; Genomic_DNA.
DR   RefSeq; WP_035689535.1; NZ_VXDA01000167.1.
DR   STRING; 728.VY92_01485; -.
DR   GeneID; 66257262; -.
DR   KEGG; apag:EIA51_00900; -.
DR   KEGG; apag:EIA51_10870; -.
DR   eggNOG; COG0050; Bacteria.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000254620; Unassembled WGS sequence.
DR   Proteomes; UP000503595; 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: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}.
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;  43428 MW;  03E05B14CE5A3C5A CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKHY GGSARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
     GDAQWEEKIL ELANHLDTYI PEPERAIDQP FLLPIEDVFS ISGRGTVVTG RVERGIIRTG
     DEVEIVGIKE TAKTTVTGVE MFRKLLDEGR AGENIGALLR GTKREEIERG QVLAKPGSIT
     PHTDFESEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT
     VSLIHPIAMD QGLRFAIREG GRTVGAGVVA KIIK
//
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