GenomeNet

Database: UniProt/SWISS-PROT
Entry: EFTU_EUBE2
LinkDB: EFTU_EUBE2
Original site: EFTU_EUBE2 
ID   EFTU_EUBE2              Reviewed;         397 AA.
AC   C4Z2R9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   22-NOV-2017, entry version 52.
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};
GN   OrderedLocusNames=EUBELI_00288;
OS   Eubacterium eligens (strain ATCC 27750 / VPI C15-48).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=515620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27750 / VPI C15-48;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of
RT   its two dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {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; CP001104; ACR71324.1; -; Genomic_DNA.
DR   RefSeq; WP_012738561.1; NC_012778.1.
DR   ProteinModelPortal; C4Z2R9; -.
DR   SMR; C4Z2R9; -.
DR   STRING; 515620.EUBELI_00288; -.
DR   PRIDE; C4Z2R9; -.
DR   EnsemblBacteria; ACR71324; ACR71324; EUBELI_00288.
DR   KEGG; eel:EUBELI_00288; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000001476; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
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;
KW   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    397       Elongation factor Tu.
FT                                /FTId=PRO_1000203008.
FT   DOMAIN       10    206       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      82     86       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     137    140       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       61     65       G2. {ECO:0000250}.
FT   REGION       82     85       G3. {ECO:0000250}.
FT   REGION      137    140       G4. {ECO:0000250}.
FT   REGION      175    177       G5. {ECO:0000250}.
SQ   SEQUENCE   397 AA;  43997 MW;  B0543F84E8AE2EC9 CRC64;
     MAKAKFERTK PHCNIGTIGH VDHGKTTLTA AITKTLHERL GTGEAVAFEN IDKAPEERER
     GITISTAHVE YETEKRHYAH VDCPGHADYV KNMITGAAQM DAGILVVAAT DGVMAQTREH
     ILLARQVGVP YIVVFMNKCD MVDDPELLEL VDMEIRELLN EYGFPGDDTP IIQGSALKAL
     EDPNSEWGDK ILELMHTIDE YVPDPERDTD KPFLMPVEDV FSITGRGTVA TGRVERGVLH
     VNEEVEIVGI HEDIRKVVVT GIEMFRKLLD EAQPGDNIGA LLRGVQRDEI QRGQVLCKPG
     SITPHHKFTA QVYVLTKDEG GRHTPFFNNY RPQFYFRTTD VTGVCELPAG TEMCMPGDNV
     EMTVELIHNV AMEQGLRFAI REGGRTVGSG AVATIIE
//
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