EFTU_META1
ID EFTU_META1 Reviewed; 397 AA.
AC B3PMU1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=MARTH_orf525;
OS Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=243272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=158L3-1;
RX PubMed=18573899; DOI=10.1128/iai.00516-08;
RA Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA Loraine A.E.;
RT "Genome of Mycoplasma arthritidis.";
RL Infect. Immun. 76:4000-4008(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; CP001047; ACF07343.1; -; Genomic_DNA.
DR RefSeq; WP_012498300.1; NC_011025.1.
DR AlphaFoldDB; B3PMU1; -.
DR SMR; B3PMU1; -.
DR STRING; 243272.MARTH_orf525; -.
DR PRIDE; B3PMU1; -.
DR EnsemblBacteria; ACF07343; ACF07343; MARTH_orf525.
DR KEGG; mat:MARTH_orf525; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_14; -.
DR OMA; EGDKEWG; -.
DR OrthoDB; 621774at2; -.
DR Proteomes; UP000008812; 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; Reference proteome.
FT CHAIN 1..397
FT /note="Elongation factor Tu"
FT /id="PRO_1000095078"
FT DOMAIN 10..207
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 177..179
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 397 AA; 43700 MW; 6CE33737F1D854EB CRC64;
MAKLDFDRSK PHVNIGTIGH VDHGKTTLTA AIATVLSKKG LSEARDYASI DNAPEEKARG
ITINTSHIEY NSEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLAKQVGVPK IVVFLNKIDM FKDDEREEMV GLVEMDVRGL LSEYGFDGDN APVIAGSALK
ALQGDPKYED IIMELVQAVD DYIDEPKRET DKPFLMAIED VFTITGRGTV ATGRVERGVL
QLNEEVEIVG IKPTKKTVVT GIEMFRKNLK QAQAGDNAGL LLRGVERTEI ERGQVLAKPK
TIIPHTEFEA TVYVLKKEEG GRHTPFFQNY KPQFYFRTTD VTGGIKFQDG REMVMPGDNV
QFTVTLISPI AVEEGTKFSI REGGRTVGAG SVTKIIK