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Database: UniProt/TrEMBL
Entry: A0A1D7R4I5_PASMD
LinkDB: A0A1D7R4I5_PASMD
Original site: A0A1D7R4I5_PASMD 
ID   A0A1D7R4I5_PASMD        Unreviewed;       394 AA.
AC   A0A1D7R4I5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   30-AUG-2017, entry version 8.
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:AON58712.1};
GN   ORFNames=A6J89_04925 {ECO:0000313|EMBL:OQV94235.1}, A6J89_07005
GN   {ECO:0000313|EMBL:OQV94619.1}, AZI96_08250
GN   {ECO:0000313|EMBL:AON58712.1}, AZI96_10380
GN   {ECO:0000313|EMBL:AON59109.1};
OS   Pasteurella multocida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=747 {ECO:0000313|EMBL:AON58712.1, ECO:0000313|Proteomes:UP000094478};
RN   [1] {ECO:0000313|EMBL:AON58712.1, ECO:0000313|Proteomes:UP000094478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm-3 {ECO:0000313|EMBL:AON58712.1,
RC   ECO:0000313|Proteomes:UP000094478};
RA   Wang Z., Kong L.;
RT   "Evaluation of Aminoglycoside Resistance Genes expression and
RT   Mutations in Ribosomal Protein S5 among Drug Susceptible and Drug
RT   Resistant Strains of Pasteurella multocida from China.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OQV94235.1, ECO:0000313|Proteomes:UP000192530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_261 {ECO:0000313|EMBL:OQV94235.1,
RC   ECO:0000313|Proteomes:UP000192530};
RA   Minogue T., Wolcott M., Wasieloski L., Jaissle J., Tallon L.,
RA   Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S.,
RA   Nadendla S., Geyer C., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx
RT   tests.";
RL   Submitted (JUL-2016) 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; CP014618; AON58712.1; -; Genomic_DNA.
DR   EMBL; CP014618; AON59109.1; -; Genomic_DNA.
DR   EMBL; NBTJ01000001; OQV94235.1; -; Genomic_DNA.
DR   EMBL; NBTJ01000001; OQV94619.1; -; Genomic_DNA.
DR   RefSeq; WP_005751979.1; NZ_NBTJ01000001.1.
DR   SMR; A0A1D7R4I5; -.
DR   EnsemblBacteria; AON58712; AON58712; AZI96_08250.
DR   EnsemblBacteria; AON59109; AON59109; AZI96_10380.
DR   GeneID; 29389059; -.
DR   KEGG; pmul:DR93_190; -.
DR   KEGG; pmul:DR93_608; -.
DR   PATRIC; fig|747.135.peg.185; -.
DR   KO; K02358; -.
DR   Proteomes; UP000094478; Chromosome.
DR   Proteomes; UP000192530; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
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:UP000094478,
KW   ECO:0000313|Proteomes:UP000192530};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AON58712.1};
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 (guanine nucleotide-binding).
FT                                {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;  43353 MW;  0C704405CF5E9A4C CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKHY GGAARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALQALN
     GVAEWEEKIL ELANHLDTYI PEPQRAIDQP FLLPIEDVFS ISGRGTVVTG RVERGIIRTG
     EEVEIVGIKA TTKTTVTGVE MFRKLLDEGR AGENVGALLR GTKREEIERG QVLAKPGSIT
     PHTDFESEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT
     VSLIHPIAMD QGLRFAIREG GRTVGAGVVA KIIK
//
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