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Database: UniProt/TrEMBL
Entry: A0A109WI72_9FIRM
LinkDB: A0A109WI72_9FIRM
Original site: A0A109WI72_9FIRM 
ID   A0A109WI72_9FIRM        Unreviewed;       395 AA.
AC   A0A109WI72;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   28-MAR-2018, entry version 14.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118, ECO:0000256|RuleBase:RU004061};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:AME03999.1};
GN   ORFNames=AXE86_07875 {ECO:0000313|EMBL:AME03999.1};
OS   Selenomonas sp. oral taxon 136.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales;
OC   Selenomonadaceae; Selenomonas.
OX   NCBI_TaxID=713030 {ECO:0000313|EMBL:AME03999.1};
RN   [1] {ECO:0000313|EMBL:AME03999.1, ECO:0000313|Proteomes:UP000067425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0591 {ECO:0000313|EMBL:AME03999.1,
RC   ECO:0000313|Proteomes:UP000067425};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00118}.
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DR   EMBL; CP014239; AME03999.1; -; Genomic_DNA.
DR   RefSeq; WP_061946124.1; NZ_CP014239.1.
DR   EnsemblBacteria; AME03999; AME03999; AXE86_07875.
DR   KEGG; selo:AXE86_07875; -.
DR   KO; K02358; -.
DR   Proteomes; UP000067425; 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 {ECO:0000313|Proteomes:UP000067425};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AME03999.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   DOMAIN       10    204       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   395 AA;  43363 MW;  BF9C61AFA131D7EE CRC64;
     MAKEKFNRSK PHVNIGTIGH VDHGKTTLTA AITKVLSEKG YAKFEDYADI DKAPEERERG
     ITINTAHVEY ETDKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA IVVFLNKVDQ VDDPELLELV EMEVRELLSS YDFPGDEIPV IAGSALKALE
     GDDAMKAKIL ELMDAVDDYI PTPTRDTDKP FLMPVEDVFT ITGRGTVATG RVERGELKLN
     DTVEIVGLQD QARSTVVTGI EMFRKLLDSA VAGDNIGALL RGVDRKDIER GQVLAKPGSI
     NPHTKFKAQV YVLTKEEGGR HTPFFTNYRP QFYFRTTDVT GVVRLPEGTE MVMPGDNVEM
     EVELITPIAI EQGLRFAIRE GGHTVGAGRV TAIEG
//
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