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Database: UniProt/TrEMBL
Entry: A0A193K9C2_9VIBR
LinkDB: A0A193K9C2_9VIBR
Original site: A0A193K9C2_9VIBR 
ID   A0A193K9C2_9VIBR        Unreviewed;       394 AA.
AC   A0A193K9C2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
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   ORFNames=A6E01_01250 {ECO:0000313|EMBL:ANO31915.1};
OS   Vibrio breoganii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=553239 {ECO:0000313|EMBL:ANO31915.1, ECO:0000313|Proteomes:UP000092018};
RN   [1] {ECO:0000313|EMBL:ANO31915.1, ECO:0000313|Proteomes:UP000092018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FF50 {ECO:0000313|EMBL:ANO31915.1,
RC   ECO:0000313|Proteomes:UP000092018};
RA   Hehemann J.-H., Arevalo P., Datta M.S., Yu X., Corzett C.,
RA   Henschel A., Preheim S.P., Timberlake S., Alm E.J., Polz M.F.;
RT   "Adaptive Radiation by Waves of Gene Transfer Leads to Fine-Scale
RT   Resource Partitioning in Marine Microbes.";
RL   Submitted (JUN-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; CP016177; ANO31915.1; -; Genomic_DNA.
DR   RefSeq; WP_065209416.1; NZ_CP016177.1.
DR   EnsemblBacteria; ANO31915; ANO31915; A6E01_01250.
DR   KEGG; vbr:A6E01_01250; -.
DR   KO; K02358; -.
DR   Proteomes; UP000092018; Chromosome 1.
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:UP000092018};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ANO31915.1};
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    204       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   394 AA;  43278 MW;  492AA074908BA722 CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AICTTLSKVY GGEAKDFASI DNAPEERERG
     ITIATSHVEY DTPDRHYAHV DCPGHADYVK NMITGAAQMD GGILVVAATD GPMPQTREHI
     LLGRQVGIPY IIVFMNKCDM VDDEELLELV EMEVRELLSE YDYPGDDLPV IQGSALGALN
     GEKQWEDKIV ELAEALDSYI PLPERAVDLP FLLPIEDVFS IQGRGTVVTG RIERGILRVG
     DEVEIVGIKE TTLTTCTGVE MFRKLLDEGR AGENVGALLR GTKRDDVERG QVLAAKGSIN
     PHTKFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG DITLPEGVEM VMPGDNVQMT
     VELIAPIAMD EGLRFAIREG GRTVGAGVVA KIFD
//
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