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Database: UniProt/TrEMBL
Entry: A0A160BN27_9PROT
LinkDB: A0A160BN27_9PROT
Original site: A0A160BN27_9PROT 
ID   A0A160BN27_9PROT        Unreviewed;       396 AA.
AC   A0A160BN27;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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:ANA13475.1};
GN   ORFNames=WG31_05170 {ECO:0000313|EMBL:ANA13475.1};
OS   Acetobacter sp. SLV-7.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=1633874 {ECO:0000313|EMBL:ANA13475.1, ECO:0000313|Proteomes:UP000076595};
RN   [1] {ECO:0000313|EMBL:ANA13475.1, ECO:0000313|Proteomes:UP000076595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLV-7 {ECO:0000313|EMBL:ANA13475.1,
RC   ECO:0000313|Proteomes:UP000076595};
RA   Cho G.Y., Jeon C.O.;
RT   "Genome study of Acetobacter sp. SLV-7.";
RL   Submitted (MAR-2015) 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; CP011120; ANA13475.1; -; Genomic_DNA.
DR   RefSeq; WP_006116052.1; NZ_CP011120.1.
DR   EnsemblBacteria; ANA13475; ANA13475; WG31_05170.
DR   KEGG; asv:WG31_05170; -.
DR   PATRIC; fig|1633874.3.peg.1125; -.
DR   KO; K02358; -.
DR   Proteomes; UP000076595; 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:UP000076595};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ANA13475.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:ANA13475.1};
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;  43253 MW;  2B20DB80F2625D8C CRC64;
     MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKTLAKKG GAEFKAYDQI DAAPEERARG
     ITISTAHVEY ETDKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFLNKVDQ VDDPELLELV EMEVRELLSS YQFPGDDVPI IKGSALVTLE
     DGDPEIGENR VRDLMDAVDA YIPQPERPVD RPFLMPIEDV FSISGRGTVV TGRVERGVIN
     VGDEIEIVGL KPTTKTTVTG VEMFRKLLDR GEAGDNIGAL LRGTKREDVE RGQVLAKPGS
     ITPHKKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVHLPEGT EMVMPGDNCA
     MEVELIAPIA MDEGLRFAIR EGGRTVGAGV VSSIIE
//
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