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Database: UniProt/TrEMBL
Entry: A0A149T2S5_9PROT
LinkDB: A0A149T2S5_9PROT
Original site: A0A149T2S5_9PROT 
ID   A0A149T2S5_9PROT        Unreviewed;       396 AA.
AC   A0A149T2S5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 9.
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:KXV46251.1};
GN   ORFNames=A0U94_08945 {ECO:0000313|EMBL:AQS91086.1}, AD945_14855
GN   {ECO:0000313|EMBL:KXV46251.1};
OS   Gluconobacter albidus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=318683 {ECO:0000313|EMBL:KXV46251.1, ECO:0000313|Proteomes:UP000075636};
RN   [1] {ECO:0000313|EMBL:KXV46251.1, ECO:0000313|Proteomes:UP000075636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 1768 {ECO:0000313|EMBL:KXV46251.1,
RC   ECO:0000313|Proteomes:UP000075636};
RA   Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT   "Improved classification and identification of acetic acid bacteria
RT   using matrix-assisted laser desorption/ionization time-of-flight mass
RT   spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are
RT   later heterotypic synonyms of Gluconobacter japonicus and
RT   Gluconobacter oxydans, respectively.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AQS91086.1, ECO:0000313|Proteomes:UP000188565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMW2.1191 {ECO:0000313|EMBL:AQS91086.1,
RC   ECO:0000313|Proteomes:UP000188565};
RA   Brandt J., Jakob F., Vogel R.F.;
RT   "Acetic acid bacteria sequencing.";
RL   Submitted (MAR-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; CP014689; AQS91086.1; -; Genomic_DNA.
DR   EMBL; LHZR01000113; KXV46251.1; -; Genomic_DNA.
DR   RefSeq; WP_062029287.1; NZ_LHZR01000113.1.
DR   EnsemblBacteria; KXV38341; KXV38341; AD941_06360.
DR   EnsemblBacteria; KXV46251; KXV46251; AD945_14855.
DR   KEGG; gal:A0U94_08945; -.
DR   PATRIC; fig|318683.5.peg.3191; -.
DR   KO; K02358; -.
DR   Proteomes; UP000075636; Unassembled WGS sequence.
DR   Proteomes; UP000188565; 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.
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:UP000075636,
KW   ECO:0000313|Proteomes:UP000188565};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:KXV46251.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:KXV46251.1};
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;  42922 MW;  1845C3D827AED2EB CRC64;
     MAKAKFERTK PHCNIGTIGH VDHGKTSLTA AITKVLAKSG GATFSAYDQI DKAPEERARG
     ITISTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFLNKVDQ VDDPELLELV EMEVRELLSS YQFPGDDIPI VKGSALVTLE
     DGDAAIGEDR VLELMTQVDA YIPQPERPVD RPFLMPIEDV FSISGRGTVV TGRVERGVVN
     VGDEVEIIGL KDTIKTTVTG VEMFRKLLDR GEAGDNIGAL VRGTKREDVE RGQVLAKPGS
     ITPHKNFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVTLPEGT EMVMPGDNVA
     MDVELIAPIA MDEGLRFAIR EGGRTVGAGV VSSITA
//
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