EFTU_MESH2
ID EFTU_MESH2 Reviewed; 402 AA.
AC Q600B6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=mhp540;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(2004).
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; AE017332; AAV27941.1; -; Genomic_DNA.
DR RefSeq; WP_011206373.1; NC_006360.1.
DR AlphaFoldDB; Q600B6; -.
DR SMR; Q600B6; -.
DR STRING; 295358.mhp540; -.
DR EnsemblBacteria; AAV27941; AAV27941; mhp540.
DR KEGG; mhy:mhp540; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_14; -.
DR OMA; EGDKEWG; -.
DR PhylomeDB; Q600B6; -.
DR Proteomes; UP000006822; 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..402
FT /note="Elongation factor Tu"
FT /id="PRO_0000337435"
FT DOMAIN 16..211
FT /note="tr-type G"
FT REGION 25..32
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 66..70
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 87..90
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 142..145
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 181..183
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 25..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 87..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 402 AA; 44094 MW; 4B28617FDBA58CA6 CRC64;
MAVVKTTGKK DFDRSKEHIN IGTIGHVDHG KTTLTAAIST VLAKKGLAEA KDYASIDAAP
EEKARGITIN TAHIEYSTDK RHYAHVDCPG HADYIKNMIT GAAQMDGAIL VVAATDGPMP
QTREHILLSK QVGVPKMVVF LNKIDLLEGE EEMVDLVEVE IRELLSSYDF DGDNTPIIRG
SARGALEGKP EWEAKVLELM DAVDSYIDSP VREMDKPFLM AVEDVFTITG RGTVATGKVE
RGQVKLNEEV EIVGYREEPK KTVITGIEMF NKNLQTAMAG DNAGVLLRGV DRKDIERGQV
IAKPKTIIPH TKFKAAIYAL KKEEGGRHTP FFKNYKPQFY FRTTDVTGGI EFEPGREMVI
PGDNVDLTVE LIAPIAVEQG TKFSIREGGR TVGAGTVTEI IK