(data stored in ACNUC30630 zone)

SWISSPROT: EFTU_TROW8

ID   EFTU_TROW8              Reviewed;         397 AA.
AC   Q83NT9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 105.
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=TW131;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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}.
DR   EMBL; BX251410; CAD66811.1; -; Genomic_DNA.
DR   RefSeq; WP_011096092.1; NC_004551.1.
DR   SMR; Q83NT9; -.
DR   EnsemblBacteria; CAD66811; CAD66811; TW131.
DR   KEGG; tws:TW131; -.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; FHNNYRP; -.
DR   BioCyc; GCF_000196075:G1EE9-136-MONOMER; -.
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   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; TF_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;
DR   PRODOM; Q83NT9.
DR   SWISS-2DPAGE; Q83NT9.
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..397
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_1000015782"
FT   DOMAIN          10..207
FT                   /note="tr-type G"
FT   NP_BIND         19..26
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   NP_BIND         84..88
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   NP_BIND         139..142
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          63..67
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          84..87
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          139..142
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          177..179
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  43508 MW;  C9C2B0E76DEB71AD CRC64;
     MAKAKFERTK PHVNIGTIGH VDHGKTTLTA AISRVLSERL PSNTNVKQDF DAIDSAPEER
     QRGITINISH IEYETEKRHY AHVDAPGHAD YIKNMITGAA QMDGAILVVA ATDGAMAQTR
     EHVLLAKQVG VPYLLVALNK ADMVSDEEIL ELVELEVREL LSTHGFDGEN VPVVRVSGLK
     ALEGDQKWGD AVMELMKAVD ESIPDPVRDR DKPFLMPIED VFTITGRGTV VTGRAERGVL
     AVNSEVEIVG IRPTQKTTVT GIEMFRKQLD EAWAGENCGL LLRGTKREDV ERGQVVVKPG
     SVTPHTKFEG KAYILSKDEG GRHNPFYSNY RPQFYFRTTD VTGVITLPEG TEMVMPGDTI
     SITVDLIQPI AMEEGLGFAI REGGRTVGAG TVVKILE
//

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