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Database: UniProt/TrEMBL
Entry: E1W2H6_HAEP3
LinkDB: E1W2H6_HAEP3
Original site: E1W2H6_HAEP3 
ID   E1W2H6_HAEP3            Unreviewed;       394 AA.
AC   E1W2H6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-SEP-2017, entry version 48.
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=PARA_04560 {ECO:0000313|EMBL:CBW14563.1}, PARA_06580
GN   {ECO:0000313|EMBL:CBW14765.1};
OS   Haemophilus parainfluenzae (strain T3T1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=862965 {ECO:0000313|EMBL:CBW14563.1, ECO:0000313|Proteomes:UP000007052};
RN   [1] {ECO:0000313|Proteomes:UP000007052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T3T1 {ECO:0000313|Proteomes:UP000007052};
RA   Crook D., Hood D., Moxon R., Parkhill J., Aslett M., Bentley S.D.;
RT   "The genome sequence of Haemophilus parainfluenzae T3T1.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBW14563.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T3T1 {ECO:0000313|EMBL:CBW14563.1};
RA   Crook D., Hood D., Moxon R., Parkhill J., Bentley S.D.;
RT   "The genome sequence of Haemophilus parainfluenzae T3T1.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CBW14563.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T3T1 {ECO:0000313|EMBL:CBW14563.1};
RA   Aslett M.;
RL   Submitted (AUG-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; FQ312002; CBW14563.1; -; Genomic_DNA.
DR   EMBL; FQ312002; CBW14765.1; -; Genomic_DNA.
DR   RefSeq; WP_005635637.1; NC_015964.1.
DR   STRING; 862965.PARA_06580; -.
DR   EnsemblBacteria; CBW14563; CBW14563; PARA_04560.
DR   EnsemblBacteria; CBW14765; CBW14765; PARA_06580.
DR   KEGG; hpr:PARA_04560; -.
DR   KEGG; hpr:PARA_06580; -.
DR   PATRIC; fig|862965.3.peg.455; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; HPAR862965:GH07-461-MONOMER; -.
DR   BioCyc; HPAR862965:GH07-667-MONOMER; -.
DR   Proteomes; UP000007052; 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:UP000007052};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CBW14563.1};
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;  43336 MW;  C237AB206F3CF4FC 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
     DEVEIVGIKP TAKTTVTGVE MFRKLLDEGR AGENIGALLR GTKREEIERG QVLAKPGSIT
     PHTDFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT
     VSLIHPIAMD QGLRFAIREG GRTVGAGVVA KIIK
//
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