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Database: UniProt/TrEMBL
Entry: D3NS24_AZOS1
LinkDB: D3NS24_AZOS1
Original site: D3NS24_AZOS1 
ID   D3NS24_AZOS1            Unreviewed;       396 AA.
AC   D3NS24;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-SEP-2017, entry version 47.
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=tufA {ECO:0000313|EMBL:BAI71203.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=AZL_005650 {ECO:0000313|EMBL:BAI71203.1}, AZL_005790
GN   {ECO:0000313|EMBL:BAI71217.1};
OS   Azospirillum sp. (strain B510).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI71203.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI71203.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI71203.1,
RC   ECO:0000313|Proteomes:UP000002040};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M.,
RA   Katoh M., Nakazaki N., Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte
RT   Azospirillum sp. B510.";
RL   DNA Res. 17:37-50(2010).
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; AP010946; BAI71203.1; -; Genomic_DNA.
DR   EMBL; AP010946; BAI71217.1; -; Genomic_DNA.
DR   RefSeq; WP_012973190.1; NC_013854.1.
DR   STRING; 137722.AZL_005790; -.
DR   EnsemblBacteria; BAI71203; BAI71203; AZL_005650.
DR   EnsemblBacteria; BAI71217; BAI71217; AZL_005790.
DR   KEGG; azl:AZL_005650; -.
DR   KEGG; azl:AZL_005790; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000002040; 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.
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:UP000002040};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:BAI71203.1};
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    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;  43025 MW;  6E15FCA1738BAFC3 CRC64;
     MAKAKFERNK PHCNVGTIGH VDHGKTSLTA AITKVLAESG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETTNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFMNKVDM VDDPELLELV ELEVRELLSS YQFPGDDIPI TKGSALCALE
     DRQPEIGRDA VLALMQTVDE YIPQPERPKD RPFLMPIEDV FSISGRGTVV TGRVERGIVK
     VGDEVEIVGL KATVKTTVTG VEMFRKLLDS GEAGDNIGAL LRGTKREDVE RGQVLAKPGS
     ITPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGMVSLPEGV EMVMPGDNVA
     MEVALIAPIA MDEGLRFAIR EGGRTVGAGV VAKIVE
//
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