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Database: UniProt/TrEMBL
Entry: A0A077LJ77_9PSED
LinkDB: A0A077LJ77_9PSED
Original site: A0A077LJ77_9PSED 
ID   A0A077LJ77_9PSED        Unreviewed;       397 AA.
AC   A0A077LJ77;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   05-JUL-2017, entry version 18.
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_2 {ECO:0000313|EMBL:BAP41894.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=PSCI_1192 {ECO:0000313|EMBL:BAP41894.1};
OS   Pseudomonas sp. StFLB209.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP41894.1, ECO:0000313|Proteomes:UP000031652};
RN   [1] {ECO:0000313|Proteomes:UP000031652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StFLB209 {ECO:0000313|Proteomes:UP000031652};
RA   Morohoshi T., Kato T., Someya N., Ikeda T.;
RT   "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing
RT   Pseudomonas sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL   Genome Announc.2:e01037-14(2014).
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; AP014637; BAP41894.1; -; Genomic_DNA.
DR   RefSeq; WP_045484144.1; NZ_AP014637.1.
DR   EnsemblBacteria; BAP41894; BAP41894; PSCI_1192.
DR   KEGG; pses:PSCI_1192; -.
DR   KO; K02358; -.
DR   Proteomes; UP000031652; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
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:UP000031652};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:BAP41894.1};
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:UP000031652}.
FT   DOMAIN       10    207       Tr-type G (guanine nucleotide-binding).
FT                                {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   397 AA;  43529 MW;  A689AB2A71F68730 CRC64;
     MAKEKFERNK PHVNVGTIGH VDHGKTTLTA ALTRVCSEVF GSAKVDFDKI DSAPEEKARG
     ITINTAHVEY DSSVRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKADM VDDAELLELV EMEVRDLLST YDFPGDDTPI IIGSALMALN
     GQDDNEMGTS AVKKLVETLD SYIPEPERAI DKTFLMPIED VFSISGRGTV VTGRVERGIV
     RIQEEVEIVG LRDTTKTTCT GVEMFRKLLD EGRAGENCGV LLRGTKRDDV ERGQVLAKPG
     TIKPHTKFVA EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGNCELPEG VEMVMPGDNI
     QMEVTLIKPI AMEDGLRFAI REGGRTVGAG VVAKIIA
//
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