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Database: UniProt/TrEMBL
Entry: A0A168Y0B0_9PROT
LinkDB: A0A168Y0B0_9PROT
Original site: A0A168Y0B0_9PROT 
ID   A0A168Y0B0_9PROT        Unreviewed;       396 AA.
AC   A0A168Y0B0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-NOV-2017, entry version 11.
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:ANC90727.1};
GN   ORFNames=A6A40_01765 {ECO:0000313|EMBL:ANC90727.1};
OS   Azospirillum humicireducens.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC90727.1, ECO:0000313|Proteomes:UP000077405};
RN   [1] {ECO:0000313|EMBL:ANC90727.1, ECO:0000313|Proteomes:UP000077405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC90727.1,
RC   ECO:0000313|Proteomes:UP000077405};
RX   PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA   Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT   "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium
RT   isolated from a microbial fuel cell.";
RL   Int. J. Syst. Evol. Microbiol. 63:2618-2624(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; CP015285; ANC90727.1; -; Genomic_DNA.
DR   RefSeq; WP_063633859.1; NZ_CP015285.1.
DR   EnsemblBacteria; ANC90727; ANC90727; A6A40_01765.
DR   KEGG; ahu:A6A40_01765; -.
DR   KO; K02358; -.
DR   Proteomes; UP000077405; 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:UP000077405};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ANC90727.1};
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:UP000077405}.
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;  42984 MW;  BF0143CE85FE8AAA CRC64;
     MAKAKFERNK PHCNVGTIGH VDHGKTSLTA AITKVLAESG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETTNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFMNKVDM VDDPELLELV ELEVRELLSS YQFPGDDIPI TKGSALCALE
     DRSPEIGRDA VLALMKTVDE YIPQPERPKD RPFLMPIEDV FSISGRGTVV TGRVERGIVK
     VGDEVEIVGL KATVKTTVTG VEMFRKLLDS GEAGDNIGAL LRGTKREDVE RGQVLAKPGS
     ITPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGMVSLPEGV EMVMPGDNVA
     MEVALIAPIA MDEGLRFAIR EGGRTVGAGV VAKIVE
//
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