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Database: UniProt/TrEMBL
Entry: D1C478_SPHTD
LinkDB: D1C478_SPHTD
Original site: D1C478_SPHTD 
ID   D1C478_SPHTD            Unreviewed;       399 AA.
AC   D1C478;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   22-NOV-2017, entry version 56.
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=Sthe_1611 {ECO:0000313|EMBL:ACZ39045.1};
OS   Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC   Bacteria; Chloroflexi; Sphaerobacteridae; Sphaerobacterales;
OC   Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX   NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ39045.1, ECO:0000313|Proteomes:UP000002027};
RN   [1] {ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20745 / S 6022 {ECO:0000313|Proteomes:UP000002027};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., LaButti K.M., Clum A., Sun H.I.,
RA   Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Markowitz V., Cheng J.F., Hugenholtz P., Woyke T., Wu D.,
RA   Steenblock K., Schneider S., Pukall R., Goeker M., Klenk H.P.,
RA   Eisen J.A.;
RT   "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ39045.1, ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20745 / S 6022 {ECO:0000313|Proteomes:UP000002027};
RX   PubMed=21304676;
RA   Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A.,
RA   Tice H., Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L.,
RA   Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Munk C., Kiss H., Chain P., Han C., Brettin T., Detter J.C.,
RA   Schuler E., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Desulfohalobium retbaense type strain
RT   (HR(100)).";
RL   Stand. Genomic Sci. 2:38-48(2010).
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; CP001823; ACZ39045.1; -; Genomic_DNA.
DR   RefSeq; WP_012872092.1; NC_013523.1.
DR   STRING; 479434.Sthe_1611; -.
DR   EnsemblBacteria; ACZ39045; ACZ39045; Sthe_1611.
DR   KEGG; sti:Sthe_1611; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000002027; Chromosome 1.
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:UP000002027};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ACZ39045.1};
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:UP000002027}.
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;  43712 MW;  E8E1CCA6F92B7708 CRC64;
     MAKQKFERTK PHVNIGTIGH VDHGKTTTTA AITKVLALKG GASFRSFDSI DNAPEERQRG
     ITIAISHVEY ETEKRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSAPD GPMPQTREHI
     LLARQVEVPA MVVFLNKVDM MDDPELLELV ELEVRELLSQ YGFPGDEVPI VRGSALAALE
     SSSQDPNAPE YAPILELMQA VDDYIPTPQR AVDQPFLMPI EDVFGIKGRG TVVTGRIERG
     RIKPGDTVEI VGLRETRQVV VTGVEMFQKT LDEGVAGDNV GCLLRGVDRD EVERGQVLAA
     PKSITPHTKF AAEVYVLSKE EGGRHTPFFP GYRPQFYIRT TDVTGEIQLP EGVEMVMPGD
     NVQMRVELIQ PVAIEAGLRF AIREGGRTVG AGVVTEIIE
//
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