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Database: UniProt/TrEMBL
Entry: A0A1P8PRX9_9SPHN
LinkDB: A0A1P8PRX9_9SPHN
Original site: A0A1P8PRX9_9SPHN 
ID   A0A1P8PRX9_9SPHN        Unreviewed;       397 AA.
AC   A0A1P8PRX9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-NOV-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   ECO:0000313|EMBL:APX65283.1};
GN   ORFNames=AV944_04870 {ECO:0000313|EMBL:APX65283.1};
OS   Sphingomonas sp. LK11.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1390395 {ECO:0000313|EMBL:APX65283.1, ECO:0000313|Proteomes:UP000187154};
RN   [1] {ECO:0000313|EMBL:APX65283.1, ECO:0000313|Proteomes:UP000187154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LK11 {ECO:0000313|EMBL:APX65283.1,
RC   ECO:0000313|Proteomes:UP000187154};
RA   Asaf S., Khan A.L., Lee I.J.;
RT   "Sphingomonas taxi complete genome sequencing.";
RL   Submitted (JAN-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; CP013916; APX65283.1; -; Genomic_DNA.
DR   RefSeq; WP_056430753.1; NZ_CP013916.1.
DR   KEGG; splk:AV944_04870; -.
DR   KO; K02358; -.
DR   Proteomes; UP000187154; 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:UP000187154};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:APX65283.1};
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    207       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   397 AA;  43074 MW;  BBD3302C877A03F6 CRC64;
     MAKAKFERNK PHLNIGTIGH VDHGKTSLTA AITKVLADNV AGNAAVDFAN IDKAPEERER
     GITISTAHVE YETEARHYAH VDCPGHADYV KNMITGAAQM DGAILVVSST DGPMPQTREH
     ILLARQVGVP AMVVFMNKVD LVDDEEILEL VELEIRELLS SYEFPGDDIP VVKGSATCAL
     SGSNDKFGKD AVLELMKQVD EYIPQPERPL DKPFMMPIED VFSISGRGTV VTGRVETGIV
     KVGEEVEIVG INNTRKTTVT GVEMFRKLLD SGQAGDNIGA LIRGVARDEV ERGQVLAKPG
     SITPHTDFQS EVYVLSKEEG GRHTPFFANY RPQFYFRTTD VTGTVELPEG TEMVMPGDNV
     ALGVKLIAPI AMDIGQRFTI REGGRTVGAG VVSSIDK
//
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