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Database: UniProt/TrEMBL
Entry: A0A024HAS5_PSEKB
LinkDB: A0A024HAS5_PSEKB
Original site: A0A024HAS5_PSEKB 
ID   A0A024HAS5_PSEKB        Unreviewed;       397 AA.
AC   A0A024HAS5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-SEP-2017, entry version 22.
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=tufa3 {ECO:0000313|EMBL:CDF81986.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufa1
GN   {ECO:0000313|EMBL:CDF81975.1};
GN   ORFNames=PKB_0606 {ECO:0000313|EMBL:CDF81975.1}, PKB_0618
GN   {ECO:0000313|EMBL:CDF81986.1};
OS   Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF81986.1, ECO:0000313|Proteomes:UP000025241};
RN   [1] {ECO:0000313|EMBL:CDF81986.1, ECO:0000313|Proteomes:UP000025241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B13 {ECO:0000313|EMBL:CDF81986.1,
RC   ECO:0000313|Proteomes:UP000025241};
RA   Linke B.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDF81986.1, ECO:0000313|Proteomes:UP000025241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B13 {ECO:0000313|EMBL:CDF81986.1,
RC   ECO:0000313|Proteomes:UP000025241};
RA   Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA   Roy S., Van der Meer J.R.;
RT   "Genome sequence of the 3-chlorobenzoate degrading bacterium
RT   Pseudomonas knackmussii B13 shows multiple evidence for horizontal
RT   gene transfer.";
RL   Submitted (MAY-2014) 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; HG322950; CDF81975.1; -; Genomic_DNA.
DR   EMBL; HG322950; CDF81986.1; -; Genomic_DNA.
DR   RefSeq; WP_043248914.1; NZ_HG322950.1.
DR   EnsemblBacteria; CDF81975; CDF81975; PKB_0606.
DR   EnsemblBacteria; CDF81986; CDF81986; PKB_0618.
DR   GeneID; 29896888; -.
DR   KEGG; pkc:PKB_0606; -.
DR   KEGG; pkc:PKB_0618; -.
DR   PATRIC; fig|1301098.3.peg.614; -.
DR   KO; K02358; -.
DR   Proteomes; UP000025241; 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:UP000025241};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CDF81986.1};
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:UP000025241}.
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;  43391 MW;  E9DDE5BA07A48B99 CRC64;
     MAKEKFERNK PHVNVGTIGH VDHGKTTLTA ALTKVCSETW GGSARAFDQI DNAPEEKARG
     ITINTSHVEY DSAVRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKADM VDDAELLELV EMEVRDLLST YDFPGDDTPI VIGSALMALN
     GQDDNEMGVS AVRKLVETLD AYIPEPVRAV DQPFLMPIED VFSISGRGTV VTGRVERGIV
     KVGEEIEIVG IRPTTKTTCT GVEMFRKLLD EGRAGENIGA LLRGTKREDV ERGQVLAKPG
     TIKPHTKFEC EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGNCELPEG VEMVMPGDNV
     KMVVTLIAPI AMEDGLRFAI REGGRTVGAG VVAKIFE
//
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