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Database: UniProt/TrEMBL
Entry: C0Q0C1_SALPC
LinkDB: C0Q0C1_SALPC
Original site: C0Q0C1_SALPC 
ID   C0Q0C1_SALPC            Unreviewed;       394 AA.
AC   C0Q0C1;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-SEP-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=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:ACN47598.1};
GN   OrderedLocusNames=SPC_3514 {ECO:0000313|EMBL:ACN47598.1}, SPC_3978
GN   {ECO:0000313|EMBL:ACN48046.1};
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN47598.1, ECO:0000313|Proteomes:UP000001599};
RN   [1] {ECO:0000313|EMBL:ACN47598.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RKS4594 {ECO:0000313|EMBL:ACN47598.1};
RA   Liu G.-R., Feng Y., Liu W.-Q., Liu S.-L., Zou Q.-H., Guo J.-T.,
RA   Chen F., Huang H., Tang J., Wang C.-Z., Zhang Y.-N., Wang Y.,
RA   He X.-Y., Wang L., Peng Y.-H., Li J.-Q., Xu G.-M., Hu S.-N., Li Z.-J.,
RA   Sanderson K.E., Johnston R.N.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACN47598.1, ECO:0000313|Proteomes:UP000001599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594 {ECO:0000313|EMBL:ACN47598.1,
RC   ECO:0000313|Proteomes:UP000001599};
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T.,
RA   Peng Y.-H., Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R.,
RA   Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella
RT   choleraesuis and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN47598.1; -; Genomic_DNA.
DR   EMBL; CP000857; ACN48046.1; -; Genomic_DNA.
DR   RefSeq; WP_000031748.1; NC_012125.1.
DR   ProteinModelPortal; C0Q0C1; -.
DR   SMR; C0Q0C1; -.
DR   EnsemblBacteria; ACN47598; ACN47598; SPC_3514.
DR   EnsemblBacteria; ACN48046; ACN48046; SPC_3978.
DR   KEGG; sei:SPC_3514; -.
DR   KEGG; sei:SPC_3978; -.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   Proteomes; UP000001599; 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:UP000001599};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ACN47598.1};
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}.
FT   DOMAIN       10    204       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   394 AA;  43284 MW;  75AF3393EB10D66E CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
     GDAEWEAKII ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
     EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK
     PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
     VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG
//
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