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Database: UniProt/TrEMBL
Entry: B1LWS4_METRJ
LinkDB: B1LWS4_METRJ
Original site: B1LWS4_METRJ 
ID   B1LWS4_METRJ            Unreviewed;       396 AA.
AC   B1LWS4;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-SEP-2017, entry version 77.
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   OrderedLocusNames=Mrad2831_2216 {ECO:0000313|EMBL:ACB24211.1},
GN   Mrad2831_3847 {ECO:0000313|EMBL:ACB25822.1};
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM
OS   2831).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB24211.1, ECO:0000313|Proteomes:UP000006589};
RN   [1] {ECO:0000313|EMBL:ACB24211.1, ECO:0000313|Proteomes:UP000006589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831
RC   {ECO:0000313|Proteomes:UP000006589}, and JCM 2831
RC   {ECO:0000313|EMBL:ACB24211.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) 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; CP001001; ACB24211.1; -; Genomic_DNA.
DR   EMBL; CP001001; ACB25822.1; -; Genomic_DNA.
DR   RefSeq; WP_012319185.1; NC_010505.1.
DR   ProteinModelPortal; B1LWS4; -.
DR   STRING; 426355.Mrad2831_3847; -.
DR   EnsemblBacteria; ACB24211; ACB24211; Mrad2831_2216.
DR   EnsemblBacteria; ACB25822; ACB25822; Mrad2831_3847.
DR   GeneID; 6139902; -.
DR   KEGG; mrd:Mrad2831_2216; -.
DR   KEGG; mrd:Mrad2831_3847; -.
DR   PATRIC; fig|426355.14.peg.3936; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000006589; 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:UP000006589};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ACB24211.1};
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:UP000006589}.
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;  43119 MW;  62013F50608BC4C9 CRC64;
     MGKEKFSRTK PHCNIGTIGH VDHGKTSLTA AITKVLAETG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETQNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFLNKVDM VDDEELLELV ELEVRELLSK YDFPGDDIPI TKGSALMALE
     DKEPKIGKEA VLALMATVDA YIPQPERPID MPFLMPIEDV FSISGRGTVV TGRVERGIVK
     VGEEVEIVGI RATTKTTVTG VEMFRKLLDQ GQAGDNVGVL LRGTKREDVE RGQVVCKPGS
     VKPHSKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGICTLPEGT EMVMPGDNVT
     MDVALIVPVA MEEKLRFAIR EGGRTVGAGV VAAIND
//
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