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Database: UniProt/TrEMBL
Entry: A0A0U5MHD6_9PROT
LinkDB: A0A0U5MHD6_9PROT
Original site: A0A0U5MHD6_9PROT 
ID   A0A0U5MHD6_9PROT        Unreviewed;       396 AA.
AC   A0A0U5MHD6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-MAR-2018, entry version 16.
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:CUW39141.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=XM1_2072 {ECO:0000313|EMBL:CUW39141.1}, XM1_2087
GN   {ECO:0000313|EMBL:CUW39156.1};
OS   Magnetospirillum sp. XM-1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW39141.1, ECO:0000313|Proteomes:UP000063191};
RN   [1] {ECO:0000313|EMBL:CUW39141.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=XM1 {ECO:0000313|EMBL:CUW39141.1};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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; LN997848; CUW39141.1; -; Genomic_DNA.
DR   EMBL; LN997848; CUW39156.1; -; Genomic_DNA.
DR   RefSeq; WP_068433039.1; NZ_LN997848.1.
DR   KEGG; magx:XM1_2072; -.
DR   KEGG; magx:XM1_2087; -.
DR   PATRIC; fig|1663591.3.peg.2064; -.
DR   KO; K02358; -.
DR   Proteomes; UP000063191; 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_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:UP000063191};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CUW39141.1};
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:UP000063191}.
FT   DOMAIN       10    206       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   396 AA;  43037 MW;  1C77BB3B02F4466B CRC64;
     MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKILAETG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETSNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFMNKCDM VDDPELLDLV ELEVRELLSS YDFPGDDIPI VKGSALCALE
     DKQPEIGRDA ILKLMAEVDA YIPQPERPKD KPFLMPIEDV FSISGRGTVV TGRVERGVVK
     VGEEVEIVGI KATVKTTCTG VEMFRKLLDQ GEAGDNIGAL LRGTKREDVE RGQVLAAPGS
     ITPHTKFEAE AYVLTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVELPEGT EMVMPGDNVK
     MHVTLIAPIA MDQGLRFAIR EGGRTVGAGV VAKIVE
//
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