ID EFTU_UREP2 Reviewed; 394 AA.
AC B1AJG3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=UPA3_0559;
OS Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; Ureaplasma.
OX NCBI_TaxID=505682;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA Methe B.A., Glass J., Waites K., Shrivastava S.;
RT "Genome sequence of Ureaplasma parvum serovar 3.";
RL Submitted (FEB-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: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; CP000942; ACA32727.1; -; Genomic_DNA.
DR RefSeq; WP_006688507.1; NC_010503.1.
DR AlphaFoldDB; B1AJG3; -.
DR SMR; B1AJG3; -.
DR GeneID; 29672348; -.
DR KEGG; upa:UPA3_0559; -.
DR HOGENOM; CLU_007265_0_1_14; -.
DR Proteomes; UP000002162; 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 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; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..394
FT /note="Elongation factor Tu"
FT /id="PRO_1000076117"
FT DOMAIN 10..204
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 174..176
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 394 AA; 42902 MW; 80A887B6C59883E0 CRC64;
MAKAKFERTK PHVNIGTIGH VDHGKTTLTA AISTVLAKKG QAIAQSYADV DKTPEERERG
ITINASHVEY ETKTRHYAHV DCPGHADYVK NMITGAAQMD GAILVIAASD GVMAQTKEHI
LLARQVGVPK IVVFLNKCDF MTDPDMQDLV EMEVRELLSK YGFDGDNTPV IRGSGLKALE
GDPVWEAKID ELMDAVDSWI PLPERSTDKP FLLAIEDVFT ISGRGTVVTG RVERGVLKVN
DEVEIVGLKD TQKTVVTGIE MFRKSLDQAE AGDNAGILLR GIKKEDVERG QVLVKPGSIK
PHRTFTAKVY ILKKEEGGRH TPIVSGYRPQ FYFRTTDVTG AISLPAGVDL VMPGDDVEMT
VELIAPVAIE DGSKFSIREG GKTVGHGSVI KTSN
//
