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Database: UniProt/TrEMBL
Entry: C1DKJ8_AZOVD
LinkDB: C1DKJ8_AZOVD
Original site: C1DKJ8_AZOVD 
ID   C1DKJ8_AZOVD            Unreviewed;       397 AA.
AC   C1DKJ8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-SEP-2017, entry version 66.
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:ACO76861.1};
GN   OrderedLocusNames=Avin_06090 {ECO:0000313|EMBL:ACO76861.1}, Avin_06230
GN   {ECO:0000313|EMBL:ACO76874.1};
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO76861.1, ECO:0000313|Proteomes:UP000002424};
RN   [1] {ECO:0000313|EMBL:ACO76861.1, ECO:0000313|Proteomes:UP000002424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ {ECO:0000313|EMBL:ACO76861.1}, and DJ / ATCC BAA-1303
RC   {ECO:0000313|Proteomes:UP000002424};
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K.,
RA   Hernandez J.A., Houmiel K., Imperial J., Kennedy C., Larson T.J.,
RA   Latreille P., Ligon L.S., Lu J., Maerk M., Miller N.M., Norton S.,
RA   O'Carroll I.P., Paulsen I., Raulfs E.C., Roemer R., Rosser J.,
RA   Segura D., Slater S., Stricklin S.L., Studholme D.J., Sun J.,
RA   Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., Dean D.R.,
RA   Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe
RT   specialized to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
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; CP001157; ACO76861.1; -; Genomic_DNA.
DR   EMBL; CP001157; ACO76874.1; -; Genomic_DNA.
DR   RefSeq; WP_012699289.1; NC_012560.1.
DR   ProteinModelPortal; C1DKJ8; -.
DR   STRING; 322710.Avin_06230; -.
DR   PRIDE; C1DKJ8; -.
DR   EnsemblBacteria; ACO76861; ACO76861; Avin_06090.
DR   EnsemblBacteria; ACO76874; ACO76874; Avin_06230.
DR   KEGG; avn:Avin_06090; -.
DR   KEGG; avn:Avin_06230; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000002424; 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:UP000002424};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ACO76861.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002424}.
FT   DOMAIN       10    207       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   397 AA;  43235 MW;  1D0ADBDF70547A18 CRC64;
     MAKEKFERNK PHVNVGTIGH VDHGKTTLTA ALTKVCAETW GGAARAFDQI DNAPEEKARG
     ITINTSHVEY DSATRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKADM VDDAELLELV EMEVRDLLST YDFPGDDTPI ITGSALMALE
     GKDDNGIGVS AVRKLVETLD SYIPEPVRAV DQPFLMPIED VFSISGRGTV VTGRVERGIV
     KVGEEVEIVG IRPTTKTTCT GVEMFRKLLD EGRAGENIGA LLRGTKREDV ERGQVLAKPG
     TIKPHTKFEA EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGNVELPEG VEMVMPGDNI
     KMTVTLIAPI AMEDGLRFAI REGGRTVGAG VVAKIIE
//
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