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Database: UniProt/SWISS-PROT
Entry: EFTU_METCA
LinkDB: EFTU_METCA
Original site: EFTU_METCA 
ID   EFTU_METCA              Reviewed;         396 AA.
AC   Q605B0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   05-DEC-2018, entry version 95.
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};
GN   OrderedLocusNames=MCA1059;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=MCA2374;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E.,
RA   Ravel J., Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R.,
RA   Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J.,
RA   Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S.,
RA   Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R.,
RA   Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU91598.1; -; Genomic_DNA.
DR   EMBL; AE017282; AAU92683.1; -; Genomic_DNA.
DR   RefSeq; WP_010960359.1; NC_002977.6.
DR   ProteinModelPortal; Q605B0; -.
DR   SMR; Q605B0; -.
DR   STRING; 243233.MCA2374; -.
DR   PRIDE; Q605B0; -.
DR   EnsemblBacteria; AAU91598; AAU91598; MCA2374.
DR   EnsemblBacteria; AAU92683; AAU92683; MCA1059.
DR   KEGG; mca:MCA1059; -.
DR   KEGG; mca:MCA2374; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; MCAP243233:G1G0X-1055-MONOMER; -.
DR   BioCyc; MCAP243233:G1G0X-2346-MONOMER; -.
DR   Proteomes; UP000006821; 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; 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    396       Elongation factor Tu.
FT                                /FTId=PRO_0000337434.
FT   DOMAIN       10    206       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       60     64       G2. {ECO:0000250}.
FT   REGION       81     84       G3. {ECO:0000250}.
FT   REGION      136    139       G4. {ECO:0000250}.
FT   REGION      174    176       G5. {ECO:0000250}.
SQ   SEQUENCE   396 AA;  43046 MW;  A0E5579948481763 CRC64;
     MSKEKFTRTK PHVNVGTIGH VDHGKTTLTA ALTKCMAAKF GGEFKAYDQI DAAPEERARG
     ITIATAHVEY ESAARHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPY IVVFLNKADM VDDPELLELV EMEVRELLSK YDFPGDDIPI IKGSALKALE
     GDGSEIGVPA VEALVQALDD YIPEPERAID RPFLMPIEDV FSISGRGTVV TGRVERGIIK
     VGEEIEIVGI RPTAKTTCTG VEMFRKLLDQ GQAGDNIGVL LRGTKREDVE RGQVLAKPGS
     ITPHTHFEAE IYVLSKEEGG RHTPFFNGYR PQFYFRTTDV TGAVTLPEGV EMVMPGDNVK
     IEVKLIAPIA MDEGLRFAVR EGGRTVGAGV VSKIIE
//
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