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Database: UniProt/TrEMBL
Entry: B5YFW5_THEYD
LinkDB: B5YFW5_THEYD
Original site: B5YFW5_THEYD 
ID   B5YFW5_THEYD            Unreviewed;       399 AA.
AC   B5YFW5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   22-NOV-2017, entry version 70.
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=tuf1 {ECO:0000313|EMBL:ACI20667.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tuf2
GN   {ECO:0000313|EMBL:ACI20932.1};
GN   OrderedLocusNames=THEYE_A1355 {ECO:0000313|EMBL:ACI20667.1},
GN   THEYE_A1448 {ECO:0000313|EMBL:ACI20932.1};
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 /
OS   YP87).
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae;
OC   Thermodesulfovibrio.
OX   NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI20667.1, ECO:0000313|Proteomes:UP000000718};
RN   [1] {ECO:0000313|Proteomes:UP000000718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87
RC   {ECO:0000313|Proteomes:UP000000718};
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii
RT   strain ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI20667.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 11347 {ECO:0000313|EMBL:ACI20667.1};
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ACI20667.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 11347 {ECO:0000313|EMBL:ACI20667.1};
RX   PubMed=25635016;
RA   Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA   Robb F.T., Ward N.L., Eisen J.A.;
RT   "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT   Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum
RT   Nitrospirae).";
RL   Genome Announc. 3:0-0(2015).
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; CP001147; ACI20667.1; -; Genomic_DNA.
DR   EMBL; CP001147; ACI20932.1; -; Genomic_DNA.
DR   RefSeq; WP_012545401.1; NC_011296.1.
DR   RefSeq; YP_002249163.1; NC_011296.1.
DR   RefSeq; YP_002249247.1; NC_011296.1.
DR   STRING; 289376.THEYE_A1448; -.
DR   EnsemblBacteria; ACI20667; ACI20667; THEYE_A1355.
DR   EnsemblBacteria; ACI20932; ACI20932; THEYE_A1448.
DR   GeneID; 6941698; -.
DR   GeneID; 6943334; -.
DR   KEGG; tye:THEYE_A1355; -.
DR   KEGG; tye:THEYE_A1448; -.
DR   PATRIC; fig|289376.4.peg.1322; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000000718; 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:UP000000718};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ACI20667.1};
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:UP000000718}.
FT   DOMAIN       10    209       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   399 AA;  44055 MW;  4F58D376E2A7F84D CRC64;
     MGKAKFERKK PHVNVGTIGH IDHGKTTLTA AITKYLELKG MAQYRSYDQI DNAPEEKARG
     ITINTAHVEY ETDKRHYAHV DCPGHADYIK NMITGAAQMD GSILVVAAND GPMPQTREHI
     LLARQVGVPY IVVFMNKTDM VDDPELLDLV ELEVRELLSK YGFPGDEIPI IKGSALKALE
     SSSKDPNAEE YKPIQELLDA LDSYIPEPER PIDKPFLMPI EDVFTISGRG TVVTGRVERG
     IIKVGDEVEI VGLRETRKTV ATGVEMFRKI LDEGRAGDNI GVLLRGIGKD EVERGMVLAK
     PGSITPHTKF KAEVYVLTKE EGGRHTPFFN GYRPQFYFRT TDVTGVIKLP DGVEMVMPGD
     NVNLSVELIA PIAMEEGLRF AIREGGRTVG AGVVTEVLE
//
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