EFTU_EHRRW
ID EFTU_EHRRW Reviewed; 395 AA.
AC Q5HAS0; Q5FD56;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; Synonyms=tufA;
GN OrderedLocusNames=Erum1660;
GN and
GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufB;
GN OrderedLocusNames=Erum6090, ERWE_CDS_06400;
OS Ehrlichia ruminantium (strain Welgevonden).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=254945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA Allsopp B.A.;
RT "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT tandem repeats of actively variable copy number.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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 -!- CAUTION: The equivalent of tuf1 in the CIRAD genome (PubMed:16547041,
CC AC Q5FCW3) is annotated as a frameshift version requiring 2 frameshifts
CC to produce full-length protein. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI27134.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR767821; CAH57882.1; -; Genomic_DNA.
DR EMBL; CR767821; CAH58341.1; -; Genomic_DNA.
DR EMBL; CR925678; CAI27134.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011154850.1; NC_006832.1.
DR AlphaFoldDB; Q5HAS0; -.
DR SMR; Q5HAS0; -.
DR STRING; 254945.Erum1660; -.
DR EnsemblBacteria; CAI27134; CAI27134; ERWE_CDS_06400.
DR GeneID; 56785369; -.
DR KEGG; eru:Erum1660; -.
DR KEGG; eru:Erum6090; -.
DR KEGG; erw:ERWE_CDS_06400; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_5; -.
DR BioCyc; ERUM254945:ERUM_RS00900-MON; -.
DR BioCyc; ERUM254945:ERUM_RS03305-MON; -.
DR Proteomes; UP000001021; 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..395
FT /note="Elongation factor Tu"
FT /id="PRO_0000337377"
FT DOMAIN 6..205
FT /note="tr-type G"
FT REGION 15..22
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 59..63
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 80..83
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 135..138
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 173..175
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 80..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 395 AA; 43282 MW; C2B3B98AD64B94F0 CRC64;
MVDGRKPHIN VGTIGHVDHG KTTLTAALTT VLAKRLSGEG NKSVKYDEID KAPEEKARGI
TISTAHVEYE TENRHYAHVD CPGHADYIKN MITGAAQMDA AILVVSATDG AMPQTREHIL
LAKQVGVKDI VVWMNKCDVV DDEEMLSLVE MEIRELLTKY GYPGDDIDVV KGSAVKALEE
ESADGVWSEK IMELMNALEK IDLPIREKDK PFLMSIEDVF SIPGRGTVVT GRIERGVIKV
GDKIDIVGLR DIQSTVCTGV EMFHKALDAG EAGDNAGILL RGIKKEDVER GQVLSAPGQI
HSYKGFKAEV YVLKKEEGGR HTPFFSNYQP QFYVRTTDVT GNIKLPDGVE MVMPGDNISI
EVNLDKPVAI DKGLRFAIRE GGRTIGSGII TEILE
