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Database: UniProt/TrEMBL
Entry: K7SX30_GLUOY
LinkDB: K7SX30_GLUOY
Original site: K7SX30_GLUOY 
ID   K7SX30_GLUOY            Unreviewed;       396 AA.
AC   K7SX30;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   20-JUN-2018, entry version 34.
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   ORFNames=B932_2000 {ECO:0000313|EMBL:AFW01567.1};
OS   Gluconobacter oxydans H24.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1224746 {ECO:0000313|EMBL:AFW01567.1, ECO:0000313|Proteomes:UP000000223};
RN   [1] {ECO:0000313|EMBL:AFW01567.1, ECO:0000313|Proteomes:UP000000223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H24 {ECO:0000313|EMBL:AFW01567.1,
RC   ECO:0000313|Proteomes:UP000000223};
RX   PubMed=23472221;
RA   Ge X., Zhao Y., Hou W., Zhang W., Chen W., Wang J., Zhao N., Lin J.,
RA   Wang W., Chen M., Wang Q., Jiao Y., Yuan Z., Xiong X.;
RT   "Complete Genome Sequence of the Industrial Strain Gluconobacter
RT   oxydans H24.";
RL   Genome Announc. 1:E00003-E00013(2013).
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; CP003926; AFW01567.1; -; Genomic_DNA.
DR   RefSeq; WP_007282719.1; NC_019396.1.
DR   EnsemblBacteria; AFW01567; AFW01567; B932_2000.
DR   GeneID; 29879549; -.
DR   KEGG; goh:B932_2000; -.
DR   PATRIC; fig|1224746.3.peg.1970; -.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000000223; 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:UP000000223};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118};
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    206       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   396 AA;  43013 MW;  FDF425D36CAD3416 CRC64;
     MAKAKFERTK PHCNIGTIGH VDHGKTSLTA AITKTLAKSG GAEFKAYDMI DAAPEERARG
     ITISTAHVEY ETKNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFLNKVDQ VDDPELLELV EMEVRELLSS YQFPGDDIPI VKGSALVTLE
     DGDATIGEDR VLELMEAVDT YIPQPERPVD RPFLMPIEDV FSISGRGTVV TGRVERGVVN
     VGDEVEIVGL KDTIKTTVTG VEMFRKLLDR GEAGDNIGAL VRGTKREDVE RGQVLAKPGS
     ITPHKKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVTLPEGT EMVMPGDNVA
     MDVELIAPIA MDEGLRFAIR EGGRTVGAGV VSSISA
//
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