ID EFTU_POLNA Reviewed; 396 AA.
AC A1VIP8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 22-NOV-2017, entry version 83.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118};
GN OrderedLocusNames=Pnap_0201;
GN and
GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118};
GN OrderedLocusNames=Pnap_3647;
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2;
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from
RT coal tar-contaminated sediment, reveals physiological and metabolic
RT versatility and evolution through extensive horizontal gene
RT transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC aminoacyl-tRNA to the A-site of ribosomes during protein
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
DR EMBL; CP000529; ABM35526.1; -; Genomic_DNA.
DR EMBL; CP000529; ABM38943.1; -; Genomic_DNA.
DR RefSeq; WP_011799636.1; NC_008781.1.
DR ProteinModelPortal; A1VIP8; -.
DR SMR; A1VIP8; -.
DR STRING; 365044.Pnap_3647; -.
DR PRIDE; A1VIP8; -.
DR EnsemblBacteria; ABM35526; ABM35526; Pnap_0201.
DR EnsemblBacteria; ABM38943; ABM38943; Pnap_3647.
DR KEGG; pna:Pnap_0201; -.
DR KEGG; pna:Pnap_3647; -.
DR eggNOG; ENOG4105CGV; Bacteria.
DR eggNOG; COG0050; LUCA.
DR HOGENOM; HOG000229290; -.
DR KO; K02358; -.
DR OMA; YGHIDCP; -.
DR OrthoDB; POG091H00LA; -.
DR Proteomes; UP000000644; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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_sf.
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; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1 396 Elongation factor Tu.
FT /FTId=PRO_0000337464.
FT DOMAIN 10 206 tr-type G.
FT NP_BIND 19 26 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT NP_BIND 81 85 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT NP_BIND 136 139 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT REGION 19 26 G1. {ECO:0000250}.
FT REGION 60 64 G2. {ECO:0000250}.
FT REGION 81 84 G3. {ECO:0000250}.
FT REGION 136 139 G4. {ECO:0000250}.
FT REGION 174 176 G5. {ECO:0000250}.
SQ SEQUENCE 396 AA; 42946 MW; 1489A791936A6C00 CRC64;
MAKEKFSRTK PHVNVGTIGH VDHGKTTLTA AIATVLAAKF GGEAKAYDQI DAAPEEKARG
ITINTAHVEY ETAARHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
LLARQVGVPY IIVFLNKCDM VDDAELLELV EMEVRELLDK YDFPGDDTPI IHGSAKLALE
GDKGPLGEEA IMKLADALDN YIPLPERAVD GAFLMPVEDV FSISGRGTVV TGRIERGIIK
VGEEIEIVGI ADTQKTICTG VEMFRKLLDQ GQAGDNVGIL LRGTKREDVQ RGQVLCKPGS
IKPHTHFTGE IYVLSKDEGG RHTPFFNNYR PQFYFRTTDV TGAIELPEGK EMVMPGDNVS
ITVKLINPIA MEEGLRFAIR EGGRTVGAGV VAKILA
//