EFTU_CHESB
ID EFTU_CHESB Reviewed; 391 AA.
AC Q11HA6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=Meso_1680;
GN and
GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=Meso_1826;
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX NCBI_TaxID=266779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNC1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL Submitted (JUN-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000390; ABG63075.1; -; Genomic_DNA.
DR EMBL; CP000390; ABG63219.1; -; Genomic_DNA.
DR RefSeq; WP_011581018.1; NC_008254.1.
DR AlphaFoldDB; Q11HA6; -.
DR SMR; Q11HA6; -.
DR STRING; 266779.Meso_1680; -.
DR EnsemblBacteria; ABG63075; ABG63075; Meso_1680.
DR EnsemblBacteria; ABG63219; ABG63219; Meso_1826.
DR KEGG; mes:Meso_1680; -.
DR KEGG; mes:Meso_1826; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_5; -.
DR OMA; EGDKEWG; -.
DR OrthoDB; 621774at2; -.
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..391
FT /note="Elongation factor Tu"
FT /id="PRO_0000337430"
FT DOMAIN 10..201
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 55..59
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 76..79
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 131..134
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 169..171
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 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 391 AA; 42794 MW; E6B41737CCD77AA6 CRC64;
MAKGKFERTK PHVNIGTIGH VDHGKTSLTA AITKYFGEFK AYDQIDAAPE EKARGITIST
AHVEYETENR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ
VGVPAIVVFL NKVDQVDDPE LLELVELEIR ELLSKYEFPG DDIPIVKGSA LAALEDSNKE
IGEDAVRQLM AEVDKYIPTP ERPIDQPFLM PIEDVFSISG RGTVVTGRVE RGVVKVGEEV
EIVGIRPTSK TTVTGVEMFR KLLDQGQAGD NIGALLRGID REGVERGQVL AKPGSVTPHT
KFKAEAYILT KEEGGRHTPF FTNYRPQFYF RTTDVTGVVT LPEGTEMVMP GDNVTMDVTL
IVPIAMEERL RFAIREGGRT VGAGIVASIT E