GenomeNet

Database: UniProt/TrEMBL
Entry: A0A127PYP6_9BURK
LinkDB: A0A127PYP6_9BURK
Original site: A0A127PYP6_9BURK 
ID   A0A127PYP6_9BURK        Unreviewed;       398 AA.
AC   A0A127PYP6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   28-MAR-2018, entry version 13.
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:AMP02876.1};
GN   ORFNames=CPter291_0385 {ECO:0000313|EMBL:AMP12672.1}, CPter291_0400
GN   {ECO:0000313|EMBL:AMP12686.1}, CPter91_0466
GN   {ECO:0000313|EMBL:AMP02862.1}, CPter91_0481
GN   {ECO:0000313|EMBL:AMP02876.1};
OS   Collimonas pratensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP02876.1, ECO:0000313|Proteomes:UP000074561};
RN   [1] {ECO:0000313|EMBL:AMP02876.1, ECO:0000313|Proteomes:UP000074561, ECO:0000313|Proteomes:UP000074914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter291 {ECO:0000313|EMBL:AMP12672.1,
RC   ECO:0000313|Proteomes:UP000074914}, and Ter91
RC   {ECO:0000313|EMBL:AMP02876.1, ECO:0000313|Proteomes:UP000074561};
RA   Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E.,
RA   Cankar K., Beekwilder J., van Veen A., de Boer W., van Veen J.A.,
RA   Garbeva P.;
RT   "Exploring the genomic traits of fungus-feeding bacterial genus
RT   Collimonas.";
RL   Submitted (NOV-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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP013234; AMP02862.1; -; Genomic_DNA.
DR   EMBL; CP013234; AMP02876.1; -; Genomic_DNA.
DR   EMBL; CP013236; AMP12672.1; -; Genomic_DNA.
DR   EMBL; CP013236; AMP12686.1; -; Genomic_DNA.
DR   RefSeq; WP_061936342.1; NZ_CP013236.1.
DR   EnsemblBacteria; AMP02862; AMP02862; CPter91_0466.
DR   EnsemblBacteria; AMP02876; AMP02876; CPter91_0481.
DR   EnsemblBacteria; AMP12672; AMP12672; CPter291_0385.
DR   EnsemblBacteria; AMP12686; AMP12686; CPter291_0400.
DR   GeneID; 34141462; -.
DR   KEGG; cpra:CPter91_0466; -.
DR   KEGG; cpra:CPter91_0481; -.
DR   PATRIC; fig|279113.10.peg.384; -.
DR   KO; K02358; -.
DR   Proteomes; UP000074561; Chromosome.
DR   Proteomes; UP000074914; 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:UP000074561,
KW   ECO:0000313|Proteomes:UP000074914};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AMP02876.1};
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:UP000074914}.
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   398 AA;  43263 MW;  BFFD2A5AB3531B5D CRC64;
     MAKGKFERTK PHVNVGTIGH VDHGKTTLTA AIATVLSKKF GGEAKAYDQI DAAPEEKARG
     ITINTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLSRQVGVPY IIVFLNKADM VDDEELLELV EMEVRELLTK YEFPGDDLPI IKGSAKLALE
     GDTGPLGEQA IMALAEALDT YIPTPERAVD GAFLLPVEDV FSISGRGTVV TGRVERGIVK
     VGEALQIVGI RDTQDTTCTG VEMFRKLLDQ GQAGDNVGVL LRGTKREDVE RGQVLAKPNS
     IKPHKHFTGE IYVLSKDEGG RHTPFFNNYR PQFYFRTTDV TGSIELPKDK EMVMPGDNVS
     ITVMLINPIA MEEGLRFAIR EGGRTVGAGV VAKILPDA
//
DBGET integrated database retrieval system