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Database: UniProt/TrEMBL
Entry: U5VKK1_9PSED
LinkDB: U5VKK1_9PSED
Original site: U5VKK1_9PSED 
ID   U5VKK1_9PSED            Unreviewed;       397 AA.
AC   U5VKK1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-SEP-2017, entry version 25.
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=PVLB_22940 {ECO:0000313|EMBL:AGZ37367.1}, PVLB_23005
GN   {ECO:0000313|EMBL:AGZ37380.1};
OS   Pseudomonas sp. VLB120.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=69328 {ECO:0000313|EMBL:AGZ37367.1, ECO:0000313|Proteomes:UP000017756};
RN   [1] {ECO:0000313|EMBL:AGZ37367.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VLB120 {ECO:0000313|EMBL:AGZ37367.1};
RA   Ruckert C., Koehler K.A.K., Blank L.M., Albersmeier A.,
RA   Szczepanowski R., Kalinowski J., Schmid A.;
RT   "Complete genome sequence of Pseudomonas sp. VLB120, a solvent
RT   tolaerant, styrene degrading bacterium isolated from soil.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGZ37367.1, ECO:0000313|Proteomes:UP000017756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VLB120 {ECO:0000313|EMBL:AGZ37367.1};
RX   PubMed=25128338; DOI=10.1128/AEM.01940-14;
RA   Volmer J., Neumann C., Buhler B., Schmid A.;
RT   "Engineering of Pseudomonas taiwanensis VLB120 for Constitutive
RT   Solvent Tolerance and Increased Specific Styrene Epoxidation
RT   Activity.";
RL   Appl. Environ. Microbiol. 80:6539-6548(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; CP003961; AGZ37367.1; -; Genomic_DNA.
DR   EMBL; CP003961; AGZ37380.1; -; Genomic_DNA.
DR   RefSeq; WP_023382632.1; NC_022738.1.
DR   EnsemblBacteria; AGZ37367; AGZ37367; PVLB_22940.
DR   EnsemblBacteria; AGZ37380; AGZ37380; PVLB_23005.
DR   KEGG; psv:PVLB_22940; -.
DR   KEGG; psv:PVLB_23005; -.
DR   PATRIC; fig|69328.3.peg.4569; -.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000017756; 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:UP000017756};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AGZ37367.1};
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      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;  43465 MW;  74716970242AD255 CRC64;
     MAKEKFDRSL PHVNVGTIGH VDHGKTTLTA ALTRVCSEVF GSAVVEFDKI DSAPEEKARG
     ITINTAHVEY NSNIRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKADL VDDAELLELV EMEVRDLLST YDFPGDDTPI IIGSARMALE
     GKDDNEMGTT AVKKLVETLD AYIPEPVRAV DQPFLMPIED VFSISGRGTV VTGRIERGIV
     RVQDPLEIVG LRETSTTTCT GVEMFRKLLD EGRAGENCGV LLRGTKRDDV ERGQVLVKPG
     SVKPHTKFTA EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGNCELPEG VEMVMPGDNI
     QMTVTLIKTI AMEDGLRFAI REGGRTVGAG VVAKIIE
//
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