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Database: UniProt/TrEMBL
Entry: A0A0G9MPJ3_9SPHN
LinkDB: A0A0G9MPJ3_9SPHN
Original site: A0A0G9MPJ3_9SPHN 
ID   A0A0G9MPJ3_9SPHN        Unreviewed;       391 AA.
AC   A0A0G9MPJ3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-SEP-2017, entry version 15.
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:KLE32554.1};
GN   ORFNames=AAW01_00310 {ECO:0000313|EMBL:KLE32554.1}, BMF35_a1486
GN   {ECO:0000313|EMBL:APE28315.1};
OS   Erythrobacter gangjinensis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=502682 {ECO:0000313|EMBL:KLE32554.1, ECO:0000313|Proteomes:UP000053070};
RN   [1] {ECO:0000313|EMBL:KLE32554.1, ECO:0000313|Proteomes:UP000053070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K7-2 {ECO:0000313|EMBL:KLE32554.1,
RC   ECO:0000313|Proteomes:UP000053070};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacr gangjinensis K7-2.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:APE28315.1, ECO:0000313|Proteomes:UP000183202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC1.15024 {ECO:0000313|EMBL:APE28315.1,
RC   ECO:0000313|Proteomes:UP000183202};
RA   Xu L., Wu Y.-H., Cheng H., Zhou Y.-G., Wu M., Cheng L., Xu X.-W.;
RT   "Complete genome sequence of two-chromosomal Erythrobacter
RT   gangjinensis CGMCC 1.15024T, isolated from seawater.";
RL   Submitted (NOV-2016) 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; CP018097; APE28315.1; -; Genomic_DNA.
DR   EMBL; LBHC01000001; KLE32554.1; -; Genomic_DNA.
DR   RefSeq; WP_047005405.1; NZ_LBHC01000001.1.
DR   EnsemblBacteria; KLE32554; KLE32554; AAW01_00310.
DR   KEGG; egn:BMF35_a1486; -.
DR   PATRIC; fig|502682.8.peg.64; -.
DR   KO; K02358; -.
DR   Proteomes; UP000053070; Unassembled WGS sequence.
DR   Proteomes; UP000183202; 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.
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:UP000053070,
KW   ECO:0000313|Proteomes:UP000183202};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:KLE32554.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:KLE32554.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053070}.
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      76     80       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     131    134       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   391 AA;  42416 MW;  F38246D587C3EEDD CRC64;
     MAKEKFERNK PHCNIGTIGH VDHGKTTLTA AITKVMGSAV DFANIDKAPE ERERGITIST
     AHVEYETDAR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VNAADGPMPQ TREHILLARQ
     VGVPALVVYM NKVDQVDDEE ILELVELEVR ELLSSYDFDG DNIPIIKGSA LAALEDRDPE
     IGENSIKELM AAVDEHIPQP DRPVDQAFLM PIEDVFSISG RGTVVTGRVE TGVVNVGDEV
     EIVGIKDTTK TTVTGVEMFR KLLDSGQAGD NIGALIRGVG RDDVERGQVL AKPGTVNPHT
     EFSAEVYVLS KDEGGRHTPF FANYRPQFYF RTTDVTGEVI LPEGTEMVMP GDNVTIGVKL
     IAPIAMDEGL RFAIREGGRT VGSGVVSKIT K
//
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