GenomeNet

Database: UniProt/TrEMBL
Entry: S5J1H6_VIBPH
LinkDB: S5J1H6_VIBPH
Original site: S5J1H6_VIBPH 
ID   S5J1H6_VIBPH            Unreviewed;       394 AA.
AC   S5J1H6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-NOV-2017, entry version 33.
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:AGQ89483.1};
GN   ORFNames=M634_00330 {ECO:0000313|EMBL:AGQ89483.1}, M634_01125
GN   {ECO:0000313|EMBL:AGQ89608.1};
OS   Vibrio parahaemolyticus O1:Kuk str. FDA_R31.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=1338034 {ECO:0000313|EMBL:AGQ89483.1, ECO:0000313|Proteomes:UP000014929};
RN   [1] {ECO:0000313|EMBL:AGQ89483.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDA_R31 {ECO:0000313|EMBL:AGQ89483.1};
RG   100K Food-borne pathogen sequencing consortium;
RA   Jones J., Zhao S., Xie Y., Thao K., Dao N., Clark T.A., Boitano M.,
RA   Korlach J., Weimer B.;
RT   "100K Food-borne pathogen sequencing project.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGQ89483.1, ECO:0000313|Proteomes:UP000014929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDA_R31 {ECO:0000313|EMBL:AGQ89483.1};
RX   PubMed=25814612;
RA   Ludeke C.H., Kong N., Weimer B.C., Fischer M., Jones J.L.;
RT   "Complete Genome Sequences of a Clinical Isolate and an Environmental
RT   Isolate of Vibrio parahaemolyticus.";
RL   Genome Announc. 3:0-0(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}.
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; CP006004; AGQ89483.1; -; Genomic_DNA.
DR   EMBL; CP006004; AGQ89608.1; -; Genomic_DNA.
DR   RefSeq; WP_005480487.1; NC_021847.1.
DR   ProteinModelPortal; S5J1H6; -.
DR   SMR; S5J1H6; -.
DR   EnsemblBacteria; AGQ89483; AGQ89483; M634_00330.
DR   EnsemblBacteria; AGQ89608; AGQ89608; M634_01125.
DR   KEGG; vpf:M634_00330; -.
DR   KEGG; vpf:M634_01125; -.
DR   KO; K02358; -.
DR   Proteomes; UP000014929; Chromosome I.
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:UP000014929};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AGQ89483.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:AGQ89483.1};
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;  43152 MW;  38AE0BC6637628E1 CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AICTTLAKVY GGEAKDFASI DNAPEERERG
     ITIATSHVEY DTPSRHYAHV DCPGHADYVK NMITGAAQMD GGILVVAATD GPMPQTREHI
     LLGRQVGIPY IIVFMNKCDM VDDEELLELV EMEVRELLSE YDFPGDDLPV IQGSALGALN
     GEEQWEAKIV ELAEALDTYI PEPERAVDQP FLMPIEDVFS IQGRGTVVTG RIERGILTVG
     DEVAIVGIKD TTTTTCTGVE MFRKLLDEGR AGENVGALLR GTKRDEVERG QVLAKPGSIT
     PHTKFESEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDVTG DISLPEGVEM VMPGDNIQMV
     VELIAPIAMD EGLRFAIREG GRTVGAGVVA KIFE
//
DBGET integrated database retrieval system