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EFTS_NITEC
ID   EFTS_NITEC              Reviewed;         294 AA.
AC   Q0AEH5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE            Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
GN   Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050}; OrderedLocusNames=Neut_2034;
OS   Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101675 / C91 / Nm57;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT   eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(2007).
CC   -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC       exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC       Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_00050}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC       Rule:MF_00050}.
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DR   EMBL; CP000450; ABI60257.1; -; Genomic_DNA.
DR   RefSeq; WP_011635054.1; NC_008344.1.
DR   AlphaFoldDB; Q0AEH5; -.
DR   SMR; Q0AEH5; -.
DR   STRING; 335283.Neut_2034; -.
DR   EnsemblBacteria; ABI60257; ABI60257; Neut_2034.
DR   KEGG; net:Neut_2034; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_4; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000001966; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.479.20; -; 2.
DR   HAMAP; MF_00050; EF_Ts; 1.
DR   InterPro; IPR036402; EF-Ts_dimer_sf.
DR   InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR   InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR   InterPro; IPR018101; Transl_elong_Ts_CS.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR11741; PTHR11741; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 2.
DR   TIGRFAMs; TIGR00116; tsf; 1.
DR   PROSITE; PS01126; EF_TS_1; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis.
FT   CHAIN           1..294
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000006136"
FT   REGION          82..85
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   294 AA;  31445 MW;  E8C9EAB29867F33C CRC64;
     MAEITASMVK ELRELTGLGM MECKKALSEA GGDMKAAEDL LRIRSGAKAS KAAARIAAEG
     VISGFITVDG KQGALIEVNC ETDFVAKNED FINFAGDLAK LMVSQSVSDT ALLAEMPLAG
     GETVESVRKA LIMKLGENIS IRRGISYHAE GRLAMYLHGS RIGVMVDYSG GDEALGKDIA
     MHIAASKPVC VSSAQVPVDL LEHERQIFTA QAAESGKPAN IIEKMVEGRV TKYLAEVTLL
     GQPFVKDPEQ TVEKLLKTKS AEVSNFTLYV VGEGIERKSD DFAAEVMAQV SQSK
 
 
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