EFTU_METH1
ID EFTU_METH1 Reviewed; 397 AA.
AC P22679; D1J7I9;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=MHO_0520;
OS Metamycoplasma hominis (strain ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC
OS 10111 / PG21) (Mycoplasma hominis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=347256;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2060757; DOI=10.1016/0378-1097(91)90075-l;
RA Ladefoged S.A., Christiansen G.;
RT "Analysis of the nucleotide sequence of the Mycoplasma hominis tuf gene and
RT its flanking region.";
RL FEMS Microbiol. Lett. 63:133-139(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 6-22.
RX PubMed=1864502; DOI=10.1016/0378-1119(91)90550-u;
RA Lueneberg E., Kamla V., Hadding U., Frosch M.;
RT "Sequence and expression in Escherichia coli of a Mycoplasma hominis gene
RT encoding elongation factor Tu.";
RL Gene 102:123-127(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC 10111 / PG21;
RX PubMed=19816563; DOI=10.1371/journal.pgen.1000677;
RA Pereyre S., Sirand-Pugnet P., Beven L., Charron A., Renaudin H., Barre A.,
RA Avenaud P., Jacob D., Couloux A., Barbe V., de Daruvar A., Blanchard A.,
RA Bebear C.;
RT "Life on arginine for Mycoplasma hominis: clues from its minimal genome and
RT comparison with other human urogenital mycoplasmas.";
RL PLoS Genet. 5:E1000677-E1000677(2009).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X57136; CAA40415.1; -; Genomic_DNA.
DR EMBL; M57675; AAA25411.1; -; Genomic_DNA.
DR EMBL; FP236530; CAX37186.1; -; Genomic_DNA.
DR PIR; JH0416; JH0416.
DR RefSeq; WP_012855329.1; NC_013511.1.
DR AlphaFoldDB; P22679; -.
DR SMR; P22679; -.
DR STRING; 347256.MHO_0520; -.
DR PRIDE; P22679; -.
DR EnsemblBacteria; CAX37186; CAX37186; MHO_0520.
DR GeneID; 57139679; -.
DR KEGG; mho:MHO_0520; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_14; -.
DR OMA; EGDKEWG; -.
DR OrthoDB; 621774at2; -.
DR Proteomes; UP000002631; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..397
FT /note="Elongation factor Tu"
FT /id="PRO_0000091347"
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"
FT CONFLICT 342
FT /note="T -> A (in Ref. 2; AAA25411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 43596 MW; DD6536AF48588DF4 CRC64;
MAKLDFDRSK PHVNIGTIGH VDHGKTTLTA AIATVLAKKG LAEARDYASI DNAPEEKARG
ITINTSHIEY QTEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLARQVGVPK IVVFLNKIDM FKDDEREEMV GLVEMDVRSL LSEYGFDGDN APIIAGSALK
ALQGDPEYEK GILELMDAVD TYIEEPKRET DKPFLMAVED VFTITGRGTV ATGRVERGVL
QLNEEVEIVG LKPTKKTVVT GIEMFRKNLK EAQAGDNAGL LLRGIDRSEV ERGQVLAKPK
TIVPHTQFEA TVYVLKKEEG GRHTPFFHNY KPQFYFRTTD VTGGIEFKPG REMVVPGDNV
ELTVTLIAPI AIEEGTKFSI REGGRTVGAG SVTKILK
