EFTU_LISMO
ID EFTU_LISMO Reviewed; 395 AA.
AC Q8Y422;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA;
GN OrderedLocusNames=lmo2653;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP DEPHOSPHORYLATION BY STP.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=15813732; DOI=10.1111/j.1365-2958.2005.04551.x;
RA Archambaud C., Gouin E., Pizarro-Cerda J., Cossart P., Dussurget O.;
RT "Translation elongation factor EF-Tu is a target for Stp, a serine-
RT threonine phosphatase involved in virulence of Listeria monocytogenes.";
RL Mol. Microbiol. 56:383-396(2005).
RN [3]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=21725001; DOI=10.1128/jb.01154-10;
RA Bruck S., Personnic N., Prevost M.C., Cossart P., Bierne H.;
RT "Regulated shift from helical to polar localization of Listeria
RT monocytogenes cell wall-anchored proteins.";
RL J. Bacteriol. 193:4425-4437(2011).
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 Secreted, cell wall {ECO:0000269|PubMed:21725001}.
CC -!- INDUCTION: Equally expressed in stationary and exponential phase (at
CC protein level). {ECO:0000269|PubMed:21725001}.
CC -!- PTM: Phosphorylated on serine and/or threonine residue(s),
CC dephosphorylated by Stp. {ECO:0000269|PubMed:15813732}.
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; AL591984; CAD00866.1; -; Genomic_DNA.
DR PIR; AD1406; AD1406.
DR RefSeq; NP_466175.1; NC_003210.1.
DR RefSeq; WP_003723640.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y422; -.
DR SMR; Q8Y422; -.
DR STRING; 169963.lmo2653; -.
DR PaxDb; Q8Y422; -.
DR EnsemblBacteria; CAD00866; CAD00866; CAD00866.
DR GeneID; 61190526; -.
DR GeneID; 987166; -.
DR KEGG; lmo:lmo2653; -.
DR PATRIC; fig|169963.11.peg.2719; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_9; -.
DR OMA; EGDKEWG; -.
DR PhylomeDB; Q8Y422; -.
DR BioCyc; LMON169963:LMO2653-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 Cell wall; Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Secreted.
FT CHAIN 1..395
FT /note="Elongation factor Tu"
FT /id="PRO_0000091343"
FT DOMAIN 10..204
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 395 AA; 43342 MW; 93979D3141C00862 CRC64;
MAKEKFDRSK PHVNIGTIGH VDHGKTTLTA AITTVLAKKG YADAQAYDQI DGAPEERERG
ITISTAHVEY QTDSRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
LLSRQVGVPY IVVFMNKCDM VDDEELLELV EMEIRDLLTE YEFPGDDIPV IKGSALKALQ
GEADWEAKID ELMEAVDSYI PTPERDTDKP FMMPVEDVFS ITGRGTVATG RVERGQVKVG
DEVEVIGIEE ESKKVVVTGV EMFRKLLDYA EAGDNIGALL RGVAREDIQR GQVLAKPGSI
TPHTNFKAET YVLTKEEGGR HTPFFNNYRP QFYFRTTDVT GIVTLPEGTE MVMPGDNIEL
AVELIAPIAI EDGTKFSIRE GGRTVGAGVV SNISK
