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Database: UniProt/TrEMBL
Entry: M1F9V7_9ALTE
LinkDB: M1F9V7_9ALTE
Original site: M1F9V7_9ALTE 
ID   M1F9V7_9ALTE            Unreviewed;       398 AA.
AC   M1F9V7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   22-NOV-2017, entry version 29.
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:AFP29535.1};
GN   ORFNames=MRBBS_0597 {ECO:0000313|EMBL:AFP29535.1}, MRBBS_0608
GN   {ECO:0000313|EMBL:AFP29546.1};
OS   Marinobacter sp. BSs20148.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=490759 {ECO:0000313|EMBL:AFP29535.1, ECO:0000313|Proteomes:UP000011757};
RN   [1] {ECO:0000313|EMBL:AFP29535.1, ECO:0000313|Proteomes:UP000011757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20148 {ECO:0000313|EMBL:AFP29535.1};
RX   PubMed=23682144;
RA   Song L., Ren L., Li X., Yu D., Yu Y., Wang X., Liu G.;
RT   "Complete Genome Sequence of Marinobacter sp. BSs20148.";
RL   Genome Announc. 1:E00236-13(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}.
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DR   EMBL; CP003735; AFP29535.1; -; Genomic_DNA.
DR   EMBL; CP003735; AFP29546.1; -; Genomic_DNA.
DR   RefSeq; WP_014869911.1; NC_018268.1.
DR   EnsemblBacteria; AFP29535; AFP29535; MRBBS_0597.
DR   EnsemblBacteria; AFP29546; AFP29546; MRBBS_0608.
DR   KEGG; mbs:MRBBS_0597; -.
DR   KEGG; mbs:MRBBS_0608; -.
DR   PATRIC; fig|490759.3.peg.591; -.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000011757; 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:UP000011757};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AFP29535.1};
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:UP000011757}.
FT   DOMAIN       10    208       Tr-type G. {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;  43720 MW;  F0D6967B212E3286 CRC64;
     MSKSKFERKK PHLNVGTIGH VDHGKTTLTA ALTRVCHDVW GTGTASAFDQ IDNAPEERAR
     GITIATSHVE YDSPNRHYAH VDCPGHADYV KNMITGAAQM DGAILVCSAA DGPMPQTREH
     ILLSRQVGVP YIVVFLNKAD MVDDEELLEL VEMEVRDLLE MYDFPADDTP IITGSALMAL
     EGRDDNEMGT TAVRKLVEAL DSYIPEPERA INLPFLMPIE DVFSISGRGT VVTGRIERGI
     VKIGEEVEIV GLKDTVKTVC TGVEMFRKLL DEGRAGENVG VLLRGTKRDD VERGQVLCKP
     GSMKPHTKFE CEVYVLSKNE GGRHTPFFKG YRPQFYFRTT DVTGACELPE GVEMVMPGDN
     VKMEVTLIAP IAMEDGLRFA IREGGRTVGA GVVAKILE
//
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