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Database: UniProt/TrEMBL
Entry: M9WWA7_MANHA
LinkDB: M9WWA7_MANHA
Original site: M9WWA7_MANHA 
ID   M9WWA7_MANHA            Unreviewed;       394 AA.
AC   M9WWA7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-SEP-2017, entry version 36.
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=tufB {ECO:0000313|EMBL:AGK00661.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:AGK01207.1};
GN   ORFNames=MHH_c01580 {ECO:0000313|EMBL:AGK00661.1}, MHH_c07470
GN   {ECO:0000313|EMBL:AGK01207.1};
OS   Mannheimia haemolytica M42548.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Mannheimia.
OX   NCBI_TaxID=1316932 {ECO:0000313|EMBL:AGK00661.1, ECO:0000313|Proteomes:UP000012987};
RN   [1] {ECO:0000313|EMBL:AGK00661.1, ECO:0000313|Proteomes:UP000012987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M42548 {ECO:0000313|EMBL:AGK00661.1,
RC   ECO:0000313|Proteomes:UP000012987};
RX   PubMed=23723408;
RA   Eidam C., Poehlein A., Brenner Michael G., Kadlec K., Liesegang H.,
RA   Brzuszkiewicz E., Daniel R., Sweeney M.T., Murray R.W., Watts J.L.,
RA   Schwarz S.;
RT   "Complete Genome Sequence of Mannheimia haemolytica Strain 42548 from
RT   a Case of Bovine Respiratory Disease.";
RL   Genome Announc. 1:E00318-13(2013).
RN   [2] {ECO:0000313|EMBL:AGK00661.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M42548 {ECO:0000313|EMBL:AGK00661.1};
RX   PubMed=25239467; DOI=10.1093/jac/dku361;
RA   Eidam C., Poehlein A., Leimbach A., Michael G.B., Kadlec K.,
RA   Liesegang H., Daniel R., Sweeney M.T., Murray R.W., Watts J.L.,
RA   Schwarz S.;
RT   "Analysis and comparative genomics of ICEMh1, a novel integrative and
RT   conjugative element (ICE) of Mannheimia haemolytica.";
RL   J. Antimicrob. Chemother. 70:93-97(2015).
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; CP005383; AGK00661.1; -; Genomic_DNA.
DR   EMBL; CP005383; AGK01207.1; -; Genomic_DNA.
DR   RefSeq; WP_006249832.1; NC_021082.1.
DR   ProteinModelPortal; M9WWA7; -.
DR   EnsemblBacteria; AGK00661; AGK00661; MHH_c01580.
DR   EnsemblBacteria; AGK01207; AGK01207; MHH_c07470.
DR   GeneID; 15341369; -.
DR   KEGG; mhx:MHH_c01580; -.
DR   KEGG; mhx:MHH_c07470; -.
DR   PATRIC; fig|1316932.3.peg.153; -.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000012987; 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:UP000012987};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AGK00661.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012987}.
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;  43313 MW;  ECB5A9789FE89E4F CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKHF GGAARAFDQI DNAPEEKARG
     ITINTSHVEY DTATRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALQALN
     GVAEWEEKIL ELANHLDTYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIRTG
     DEVEIVGIKD TAKTTVTGVE MFRKLLDEGR AGENVGALLR GTKREEIERG QVLAKPGSIT
     PHTDFESEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT
     VSLIHPIAMD EGLRFAIREG GRTVGAGVVA KIIK
//
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