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Database: UniProt/TrEMBL
Entry: E1XAM7_HAEI1
LinkDB: E1XAM7_HAEI1
Original site: E1XAM7_HAEI1 
ID   E1XAM7_HAEI1            Unreviewed;       394 AA.
AC   E1XAM7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   05-JUL-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=tuf2 {ECO:0000313|EMBL:CBW28892.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=HIB_07040 {ECO:0000313|EMBL:CBW28892.1}, HIB_07620
GN   {ECO:0000313|EMBL:CBW28949.1};
OS   Haemophilus influenzae (strain 10810).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=862964 {ECO:0000313|EMBL:CBW28892.1, ECO:0000313|Proteomes:UP000008964};
RN   [1] {ECO:0000313|EMBL:CBW28892.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=10810 {ECO:0000313|EMBL:CBW28892.1};
RA   Crook D., Hood D., Moxon R., Bentley S.D., Parkhill J.;
RT   "The genome sequence of Haemophilus influenzae 10810.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10810 {ECO:0000313|Proteomes:UP000008964};
RA   Crook D., Hood D., Moxon R., Bentley S.D., Aslett M., Parkhill J.;
RT   "The genome sequence of Haemophilus influenzae 10810.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CBW28892.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=10810 {ECO:0000313|EMBL:CBW28892.1};
RA   Aslett M.;
RL   Submitted (JUL-2010) 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; FQ312006; CBW28892.1; -; Genomic_DNA.
DR   EMBL; FQ312006; CBW28949.1; -; Genomic_DNA.
DR   RefSeq; WP_005667564.1; NC_016809.1.
DR   ProteinModelPortal; E1XAM7; -.
DR   SMR; E1XAM7; -.
DR   PRIDE; E1XAM7; -.
DR   EnsemblBacteria; CBW28892; CBW28892; HIB_07040.
DR   EnsemblBacteria; CBW28949; CBW28949; HIB_07620.
DR   KEGG; hiu:HIB_07040; -.
DR   KEGG; hiu:HIB_07620; -.
DR   PATRIC; fig|862964.3.peg.726; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; HINF862964:GHI0-728-MONOMER; -.
DR   BioCyc; HINF862964:GHI0-801-MONOMER; -.
DR   Proteomes; UP000008964; Chromosome.
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:UP000008964};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118};
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;  43354 MW;  79AC25FAAF3CEE26 CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKHY GGAARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALQALN
     GVAEWEEKIL ELANHLDTYI PEPERAIDQP FLLPIEDVFS ISGRGTVVTG RVERGIIRTG
     DEVEIVGIKD TAKTTVTGVE MFRKLLDEGR AGENIGALLR GTKREEIERG QVLAKPGSIT
     PHTDFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT
     VSLIHPIAMD QGLRFAIREG GRTVGAGVVA KIIK
//
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