ID B3GYJ3_ACTP7 Unreviewed; 394 AA.
AC B3GYJ3;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 109.
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=tufB2 {ECO:0000313|EMBL:ACE62224.1};
GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufB1
GN {ECO:0000313|EMBL:ACE62193.1};
GN OrderedLocusNames=APP7_1541 {ECO:0000313|EMBL:ACE62193.1}, APP7_1572
GN {ECO:0000313|EMBL:ACE62224.1};
OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=537457 {ECO:0000313|EMBL:ACE62224.1, ECO:0000313|Proteomes:UP000001226};
RN [1] {ECO:0000313|EMBL:ACE62224.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AP76 {ECO:0000313|EMBL:ACE62224.1};
RA Linke B.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000001226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP76 {ECO:0000313|Proteomes:UP000001226};
RA Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA Tegetmeyer H., Singh M., Gerlach G.F.;
RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ACE62224.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AP76 {ECO:0000313|EMBL:ACE62224.1};
RA Buettner F., Martinez-Arias R., Goesmann A., Baltes N., Tegetmeyer H.,
RA Singh M., Gerlach G.F.;
RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL Submitted (JUN-2008) 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; CP001091; ACE62193.1; -; Genomic_DNA.
DR EMBL; CP001091; ACE62224.1; -; Genomic_DNA.
DR RefSeq; WP_009875214.1; NC_010939.1.
DR AlphaFoldDB; B3GYJ3; -.
DR SMR; B3GYJ3; -.
DR GeneID; 69418773; -.
DR KEGG; apa:APP7_1541; -.
DR KEGG; apa:APP7_1572; -.
DR PATRIC; fig|416269.6.peg.1456; -.
DR HOGENOM; CLU_007265_0_2_6; -.
DR Proteomes; UP000001226; 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}; Hydrolase {ECO:0000313|EMBL:ACE62224.1};
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; 43467 MW; 412C1B33DF29910B CRC64;
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLSKHF GGAARAFDQI DNAPEEKARG
ITINTSHVEY DTETRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALQALN
GVPEWEEKIL ELAHHLDTYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKSG
EEVEIVGIKE TTKTTVTGVE MFRKLLDEGR AGENVGALLR GTKREEIERG QVLAKPGTIT
PHTDFESEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT
VSLIHPIAMD EGLRFAIREG GRTVGAGVVA KIIK
//
