ID B7J452_ACIF2 Unreviewed; 396 AA.
AC B7J452;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 29-MAY-2013, entry version 35.
DE RecName: Full=Elongation factor Tu;
DE Short=EF-Tu;
GN Name=tuf-2; Synonyms=tuf, tuf-1; OrderedLocusNames=AFE_0311, AFE_0325;
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB
OS 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / NCIB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H.,
RA Blake R. II, Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC aminoacyl-tRNA to the A-site of ribosomes during protein
CC biosynthesis (By similarity).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-Tu/EF-1A subfamily.
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DR EMBL; CP001219; ACK77993.1; -; Genomic_DNA.
DR EMBL; CP001219; ACK78942.1; -; Genomic_DNA.
DR RefSeq; YP_002424815.1; NC_011761.1.
DR RefSeq; YP_002424828.1; NC_011761.1.
DR STRING; 243159.AFE_0325; -.
DR EnsemblBacteria; ACK77993; ACK77993; AFE_0311.
DR EnsemblBacteria; ACK78942; ACK78942; AFE_0325.
DR GeneID; 7136011; -.
DR GeneID; 7136844; -.
DR KEGG; afr:AFE_0311; -.
DR KEGG; afr:AFE_0325; -.
DR PATRIC; 20651957; VBIAciFer29821_0300.
DR eggNOG; COG0050; -.
DR HOGENOM; HOG000229290; -.
DR KO; K02358; -.
DR OMA; CEFVGYN; -.
DR ProtClustDB; PRK12735; -.
DR BioCyc; AFER243159:GH3S-311-MONOMER; -.
DR BioCyc; AFER243159:GH3S-325-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR HAMAP; MF_00118_B; EF_Tu_B; 1; -.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
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; SSF50465; Elong_init_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF50447; Translat_factor; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis.
FT NP_BIND 19 26 GTP (By similarity).
FT NP_BIND 81 85 GTP (By similarity).
FT NP_BIND 136 139 GTP (By similarity).
SQ SEQUENCE 396 AA; 43179 MW; C487F76D11C7564B CRC64;
MSKGKFERTK PHVNVGTIGH VDHGKTTLTA ALTKVLSAKF GGEIRAYDQI DNAPEERARG
ITIATSHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
LLARQVGVPY IVVFLNKADM VDDAELLELV EMEVRELLSK YEFPGDDIPV IIGSALKALE
GDQSDIGEPA IFRLADAMDS YIPMPERPVD KPFLMPIEDV FSISGRGTVV TGRIERGIVK
IGDEIEIIGI HNTAKSIVTG VEMFRKILDQ GQAGDNVGVL LRGTKKDDVE RGQVLAKPGS
IKPHTRFEAE VYVLSKEEGG RHTPFFNGYR PQFYFRTTDV TGAVELPEGV EMVMPGDNIL
FKVALIAPIA MEEGLRFAVR EGGRTVGAGV VSKVVE
//
