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Database: UniProt/TrEMBL
Entry: H8W460_MARHY
LinkDB: H8W460_MARHY
Original site: H8W460_MARHY 
ID   H8W460_MARHY            Unreviewed;       398 AA.
AC   H8W460;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   05-JUL-2017, entry version 43.
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:CCG94060.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufA
GN   {ECO:0000313|EMBL:CCG94072.1};
GN   ORFNames=MARHY0567 {ECO:0000313|EMBL:CCG94060.1}, MARHY0580
GN   {ECO:0000313|EMBL:CCG94072.1};
OS   Marinobacter hydrocarbonoclasticus ATCC 49840.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=1163748 {ECO:0000313|EMBL:CCG94060.1, ECO:0000313|Proteomes:UP000007884};
RN   [1] {ECO:0000313|EMBL:CCG94060.1, ECO:0000313|Proteomes:UP000007884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49840 {ECO:0000313|EMBL:CCG94060.1};
RX   PubMed=22689231; DOI=10.1128/JB.00500-12;
RA   Grimaud R., Ghiglione J.F., Cagnon C., Lauga B., Vaysse P.J.,
RA   Rodriguez-Blanco A., Mangenot S., Cruveiller S., Barbe V., Duran R.,
RA   Wu L.F., Talla E., Bonin P., Michotey V.;
RT   "Genome Sequence of the Marine Bacterium Marinobacter
RT   hydrocarbonoclasticus SP17, Which Forms Biofilms on Hydrophobic
RT   Organic Compounds.";
RL   J. Bacteriol. 194:3539-3540(2012).
RN   [2] {ECO:0000313|EMBL:CCG94060.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 49840 {ECO:0000313|EMBL:CCG94060.1};
RA   Genoscope - CEA;
RL   Submitted (MAR-2012) 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; FO203363; CCG94060.1; -; Genomic_DNA.
DR   EMBL; FO203363; CCG94072.1; -; Genomic_DNA.
DR   RefSeq; WP_011784245.1; NC_017067.1.
DR   ProteinModelPortal; H8W460; -.
DR   SMR; H8W460; -.
DR   PRIDE; H8W460; -.
DR   EnsemblBacteria; CCG94060; CCG94060; MARHY0567.
DR   EnsemblBacteria; CCG94072; CCG94072; MARHY0580.
DR   GeneID; 31820092; -.
DR   KEGG; mhc:MARHY0567; -.
DR   KEGG; mhc:MARHY0580; -.
DR   PATRIC; fig|2743.3.peg.540; -.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000007884; 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:UP000007884};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CCG94060.1};
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}.
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;  43663 MW;  1A5B5C16D8438A7F CRC64;
     MSKAKFERNK PHVNVGTIGH VDHGKTTLTA ALTRVCHEVW GTGESRAFDQ IDNAPEERAR
     GITIATSHVE YDSPTRHYAH VDCPGHADYV KNMITGAAQM DGAILVCSAA DGPMPQTREH
     ILLSRQVGVP FIVVFLNKAD MVDDEELLEL VEMEVRDLLS QYDFPGDDTP IITGSALMAL
     EGKDDNEMGT TAVKKLVEAL DDYIPEPERA IDQPFLMPIE DVFSISGRGT VVTGRVERGI
     IKVGDEVEIV GIRDTTKTTC TGVEMFRKLL DEGRAGENVG VLLRGTKRDD VERGQVLCVP
     GSIKPHTKFE CEVYVLSKEE GGRHTPFFKG YRPQFYFRTT DVTGSCELPE GVEMVMPGDN
     VKMTVTLIAP IAMEDGLRFA IREGGRTVGA GVVAKIIE
//
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