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Database: UniProt/TrEMBL
Entry: A0A1D9GMV3_9ALTE
LinkDB: A0A1D9GMV3_9ALTE
Original site: A0A1D9GMV3_9ALTE 
ID   A0A1D9GMV3_9ALTE        Unreviewed;       398 AA.
AC   A0A1D9GMV3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   05-JUL-2017, entry version 6.
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   ORFNames=BKP64_12455 {ECO:0000313|EMBL:AOY88919.1};
OS   Marinobacter salinus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=1874317 {ECO:0000313|EMBL:AOY88919.1, ECO:0000313|Proteomes:UP000177445};
RN   [1] {ECO:0000313|EMBL:AOY88919.1, ECO:0000313|Proteomes:UP000177445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hb8 {ECO:0000313|EMBL:AOY88919.1,
RC   ECO:0000313|Proteomes:UP000177445};
RA   Park S.-J.;
RT   "Marinobacter salinus sp. nov., a moderately halophilic bacterium
RT   isolated from a tidal flat environment.";
RL   Submitted (OCT-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; CP017715; AOY88919.1; -; Genomic_DNA.
DR   RefSeq; WP_070970532.1; NZ_CP017715.1.
DR   Proteomes; UP000177445; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
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:UP000177445};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AOY88919.1};
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:UP000177445}.
FT   DOMAIN       10    208       Tr-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      82     86       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     137    140       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   398 AA;  43568 MW;  BADD5B63F1E4A460 CRC64;
     MSKEKFDRSK PHLNVGTIGH VDHGKTTLTA ALTRVCHEVW GTGSASAFDQ IDNAPEEKAR
     GITIATSHVE YDSPTRHYAH VDCPGHADYV KNMITGAAQM DGAILVCSAA DGPMPQTREH
     ILLSRQVGVP YIVVFLNKAD MVDDEELLEL VEMEVRDLLS QYDFPGDDTP IITGSALMAL
     EGKDDNEMGT TAVKKLVEAL DDYIPEPERA IDQPFLMPIE DVFSISGRGT VVTGRVERGI
     IKVGEEVEIV GIKDTVKTTC TGVEMFRKLL DEGRAGENVG VLLRGTKRDD VERGQVLCKP
     GTIKPHTKFE CEVYVLSKEE GGRHTPFFKG YRPQFYFRTT DVTGSCELPE GVEMVMPGDN
     VKMSVTLIAP IAMEDGLRFA IREGGRTVGA GVVAKIIE
//
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