EFV_ENTFA
ID EFV_ENTFA Reviewed; 487 AA.
AC Q838U8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=NAD(+)--arginine ADP-ribosyltransferase EFV;
DE EC=2.4.2.31;
DE AltName: Full=Putative mono(ADP-ribosyl)transferase;
DE Short=mADPRT;
DE Short=mART;
DE AltName: Full=Toxin EFV;
GN OrderedLocusNames=EF_0335;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP FUNCTION AS A TOXIN, EXPRESSION IN YEAST, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLU-461 AND GLU-463.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=21170356; DOI=10.1371/journal.pcbi.1001029;
RA Fieldhouse R.J., Turgeon Z., White D., Merrill A.R.;
RT "Cholera- and anthrax-like toxins are among several new ADP-
RT ribosyltransferases.";
RL PLoS Comput. Biol. 6:E1001029-E1001029(2010).
CC -!- FUNCTION: A probable mono(ADP-ribosyl)transferase, it may ADP-
CC ribosylate Arg in target protein(s). Upon expression in yeast cells
CC causes cell death. {ECO:0000269|PubMed:21170356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142554; EC=2.4.2.31;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; AE016830; AAO80198.1; -; Genomic_DNA.
DR RefSeq; NP_814127.1; NC_004668.1.
DR RefSeq; WP_011109439.1; NZ_KE136524.1.
DR AlphaFoldDB; Q838U8; -.
DR SMR; Q838U8; -.
DR STRING; 226185.EF_0335; -.
DR EnsemblBacteria; AAO80198; AAO80198; EF_0335.
DR KEGG; efa:EF0335; -.
DR PATRIC; fig|226185.9.peg.311; -.
DR eggNOG; COG2369; Bacteria.
DR HOGENOM; CLU_041007_0_0_9; -.
DR OMA; WINEETE; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR003540; ADP-ribosyltransferase.
DR InterPro; IPR006528; Phage_head_morphogenesis_dom.
DR Pfam; PF03496; ADPrib_exo_Tox; 1.
DR Pfam; PF04233; Phage_Mu_F; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Glycosyltransferase; NAD; NADP; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Secreted; Toxin; Transferase;
KW Virulence.
FT CHAIN 1..487
FT /note="NAD(+)--arginine ADP-ribosyltransferase EFV"
FT /id="PRO_0000410944"
FT DOMAIN 315..487
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT COILED 2..51
FT /evidence="ECO:0000255"
FT ACT_SITE 394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 346..358
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 394..400
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 463
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MUTAGEN 461..463
FT /note="ESE->ASA: Restores 60% growth in yeast."
FT MUTAGEN 461
FT /note="E->A: Restores 30% growth in yeast."
FT /evidence="ECO:0000269|PubMed:21170356"
FT MUTAGEN 463
FT /note="E->A: Restores 40% growth in yeast."
FT /evidence="ECO:0000269|PubMed:21170356"
SQ SEQUENCE 487 AA; 56055 MW; 73F4677B4C1CD038 CRC64;
MSQLNKWQKE LQALQKANYQ ETDNQLFNVY RQSLIDIKKR LKVYTENAES LSFSTRLEVE
RLFSVADEIN AILQLNSPKV EKTIKGYSAK QAEQGYYGLW YTLEQSQNIA LSMPLINHDY
IMNLVNAPVA GKRLSKRLYK YRDELAQNVT NNIITGLFEG KSYAEIARWI NEETEASYKQ
ALRIARTEAG RTQSVTTQKG YEEAKELGIN IKKKWLATID KHTRRTHQEL DGKEVDVDEE
FTIRGHSAKG PRMFGVASED VNCRCTTIEV VDGISPELRK DNESKEMSEF KSYDEWYADR
IRQNESKPKP NFTELDFFGQ SDLQDDSDKW VAGLKPEQVN AMKDYTSDAF AKMNKILRNE
KYNPREKPYL VNIIQNLDDA ISKFKLKHDI ITYRGVSANE YDAILNGNVF KEFKSTSINK
KVAEDFLNFT SANKDGRVVK FLIPKGTQGA YIGTNSSMKK ESEFLLNRNL KYTVEIVDNI
LEVTILG
