GenomeNet

Database: UniProt/TrEMBL
Entry: U4KH93_9VIBR
LinkDB: U4KH93_9VIBR
Original site: U4KH93_9VIBR 
ID   U4KH93_9VIBR            Unreviewed;       394 AA.
AC   U4KH93;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   22-NOV-2017, entry version 26.
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:CCO59334.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=VIBNI_A3334 {ECO:0000313|EMBL:CCO59334.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO59334.1, ECO:0000313|Proteomes:UP000016895};
RN   [1] {ECO:0000313|EMBL:CCO59334.1, ECO:0000313|Proteomes:UP000016895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX   PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA   Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S.,
RA   Calteau A., Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT   "Comparative genomics of pathogenic lineages of Vibrio
RT   nigripulchritudo identifies virulence-associated traits.";
RL   ISME J. 7:1985-1996(2013).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; FO203526; CCO59334.1; -; Genomic_DNA.
DR   RefSeq; WP_022551812.1; NC_022528.1.
DR   EnsemblBacteria; CCO59334; CCO59334; VIBNI_A3334.
DR   GeneID; 29462478; -.
DR   KEGG; vni:VIBNI_A3334; -.
DR   PATRIC; fig|1260221.3.peg.3171; -.
DR   KO; K02358; -.
DR   Proteomes; UP000016895; 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_sf.
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:UP000016895};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CCO59334.1};
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:UP000016895}.
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;  43164 MW;  8E8425F6EA6FE5C2 CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AICTTLAKVY GGEAKDFASI DNAPEERERG
     ITIATSHVEY DTPSRHYAHV DCPGHADYVK NMITGAAQMD GGILVVAATD GPMPQTREHI
     LLGRQVGIPY IIVFMNKCDM VDDEELLELV EMEVRELLSE YEFPGDDLPV IQGSALGALN
     GEKQWEDKIV ELAEALDSYI PEPERAVDQP FLLPIEDVFS IQGRGTVVTG RIERGILTVG
     DDVEIVGIKE TTTTTCTGVE MFRKLLDEGR AGENVGALLR GTKRDEVERG QVLAAPGSIN
     PHTKFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG DIQLPEGVEM VMPGDNVQMT
     VTLIAPIAMD EGLRFAIREG GRTVGAGVVA KIFD
//
DBGET integrated database retrieval system