EFTU_PSEAE
ID EFTU_PSEAE Reviewed; 397 AA.
AC P09591; Q9HWD3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=PA4265;
GN and
GN Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=PA4277;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=3136442; DOI=10.1093/nar/16.14.7193;
RA Hughes M.A., Jones D.S.;
RT "A fragment of the Pseudomonas aeruginosa genome contains five tRNA genes,
RT four of which are linked to an EF-Tu gene.";
RL Nucleic Acids Res. 16:7193-7193(1988).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {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}.
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DR EMBL; AE004091; AAG07653.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07665.1; -; Genomic_DNA.
DR EMBL; X07950; CAA30775.1; -; Genomic_DNA.
DR PIR; F83111; F83111.
DR PIR; S01222; S01222.
DR RefSeq; NP_252955.1; NC_002516.2.
DR RefSeq; NP_252967.1; NC_002516.2.
DR RefSeq; WP_003115146.1; NZ_QZGE01000028.1.
DR PDB; 4ZV4; X-ray; 3.50 A; A/B=1-397.
DR PDBsum; 4ZV4; -.
DR AlphaFoldDB; P09591; -.
DR SMR; P09591; -.
DR IntAct; P09591; 1.
DR MINT; P09591; -.
DR STRING; 287.DR97_3633; -.
DR MoonProt; P09591; -.
DR PaxDb; P09591; -.
DR PRIDE; P09591; -.
DR EnsemblBacteria; AAG07653; AAG07653; PA4265.
DR EnsemblBacteria; AAG07665; AAG07665; PA4277.
DR GeneID; 881697; -.
DR GeneID; 881718; -.
DR KEGG; pae:PA4265; -.
DR KEGG; pae:PA4277; -.
DR PATRIC; fig|208964.12.peg.4466; -.
DR PseudoCAP; PA4265; -.
DR PseudoCAP; PA4277; -.
DR HOGENOM; CLU_007265_0_0_6; -.
DR InParanoid; P09591; -.
DR OMA; EGDKEWG; -.
DR PhylomeDB; P09591; -.
DR Proteomes; UP000002438; 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; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
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; T_Tr_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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..397
FT /note="Elongation factor Tu"
FT /id="PRO_0000091365"
FT DOMAIN 10..207
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 60..64
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 136..139
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 174..176
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 397 AA; 43370 MW; A019D5BF8EBAB942 CRC64;
MAKEKFERNK PHVNVGTIGH VDHGKTTLTA ALTKVCSDTW GGSARAFDQI DNAPEEKARG
ITINTSHVEY DSAVRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
LLSRQVGVPY IVVFLNKADM VDDAELLELV EMEVRDLLNT YDFPGDDTPI IIGSALMALE
GKDDNGIGVS AVQKLVETLD SYIPEPVRAI DQPFLMPIED VFSISGRGTV VTGRVERGII
KVQEEVEIVG IKATTKTTCT GVEMFRKLLD EGRAGENVGI LLRGTKREDV ERGQVLAKPG
TIKPHTKFEC EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGNCELPEG VEMVMPGDNI
KMVVTLIAPI AMEDGLRFAI REGGRTVGAG VVAKIIE
