LART1_LEGPH
ID LART1_LEGPH Reviewed; 303 AA.
AC Q5ZZ30;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=NAD(+)--arginine ADP-ribosyltransferase Lart1 {ECO:0000305};
DE EC=2.4.2.31 {ECO:0000269|PubMed:33476647};
DE AltName: Full=Legionella ADP-ribosyltransferase 1 {ECO:0000303|PubMed:33476647};
DE Short=Legionella ART 1 {ECO:0000303|PubMed:33476647};
DE AltName: Full=Mono-ADP-ribosyltransferase {ECO:0000303|PubMed:33476647};
DE Short=Mono-ART {ECO:0000303|PubMed:33476647};
DE Short=mART {ECO:0000303|PubMed:33476647};
GN Name=Lart1 {ECO:0000303|PubMed:33476647};
GN OrderedLocusNames=lpg0181 {ECO:0000312|EMBL:AAU26288.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=21408005; DOI=10.1371/journal.pone.0017638;
RA Zhu W., Banga S., Tan Y., Zheng C., Stephenson R., Gately J., Luo Z.Q.;
RT "Comprehensive identification of protein substrates of the Dot/Icm type IV
RT transporter of Legionella pneumophila.";
RL PLoS ONE 6:e17638-e17638(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLU-137.
RX PubMed=33476647; DOI=10.1016/j.jbc.2021.100301;
RA Black M.H., Osinski A., Park G.J., Gradowski M., Servage K.A.,
RA Pawlowski K., Tagliabracci V.S.;
RT "A Legionella effector ADP-ribosyltransferase inactivates glutamate
RT dehydrogenase.";
RL J. Biol. Chem. 296:100301-100301(2021).
CC -!- FUNCTION: ADP-ribosyltransferase that targets a specific class of
CC NAD(+)-dependent glutamate dehydrogenase (GDH) enzymes found in fungi
CC and protists, including many natural hosts of Legionella. Acts by
CC targeting a conserved arginine residue in the NAD(+)-binding pocket of
CC GDH, thereby blocking oxidative deamination of glutamate. Lart1 may
CC target amoeba GDH to prevent a conserved stress response. In vitro,
CC acts on Glud2 from the amoeba Dictyostelium discoideum (DdGluD2) and
CC yeast Gdh2p but does not act on human or Legionella GDH homologs.
CC {ECO:0000269|PubMed:33476647}.
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 Evidence={ECO:0000269|PubMed:33476647};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.22 uM for DdGluD2 {ECO:0000269|PubMed:33476647};
CC KM=1.57 uM for NAD(+) {ECO:0000269|PubMed:33476647};
CC Note=kcat is 0.11 min(-1) with DdGluD2 as substrate. kcat is 0.15
CC min(-1) with NAD(+) as substrate. {ECO:0000269|PubMed:33476647};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:33476647};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21408005}.
CC Note=Translocated into the host cell via the type IV secretion system
CC (T4SS). {ECO:0000269|PubMed:21408005}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene has no effect on bacterial
CC replication in the amoeba A.castellani. {ECO:0000269|PubMed:33476647}.
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DR EMBL; AE017354; AAU26288.1; -; Genomic_DNA.
DR RefSeq; WP_010945942.1; NC_002942.5.
DR RefSeq; YP_094235.1; NC_002942.5.
DR SMR; Q5ZZ30; -.
DR STRING; 272624.lpg0181; -.
DR PaxDb; Q5ZZ30; -.
DR PRIDE; Q5ZZ30; -.
DR EnsemblBacteria; AAU26288; AAU26288; lpg0181.
DR GeneID; 66489386; -.
DR KEGG; lpn:lpg0181; -.
DR PATRIC; fig|272624.6.peg.194; -.
DR eggNOG; ENOG5030R09; Bacteria.
DR HOGENOM; CLU_917625_0_0_6; -.
DR OMA; CFITIDP; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Glycosyltransferase; NAD; Nucleotidyltransferase; Reference proteome;
KW Secreted; Transferase; Virulence.
FT CHAIN 1..303
FT /note="NAD(+)--arginine ADP-ribosyltransferase Lart1"
FT /id="PRO_0000453644"
FT MUTAGEN 137
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:33476647"
SQ SEQUENCE 303 AA; 34911 MW; C1A77E00FFA41379 CRC64;
MYSKYPAFFL NKNIKSSSGV QFSNVVKIPS AIESLYRGDN NLTGIIFLLP TLITGVFCQN
FPEVVDIEQI RLHKLTNLSN DFHMVSMSED PQIALDWGNG CFITIDPVSF SDYIVDVHAT
FSENQLNLPG RMEREKEHVA LAVPFCSIKK ITIHNKELAN PFYLSIPQEN HEAKMELNTL
YGELISLLRK KYTQEVDEKE EQIALRTYAI RYLDFYAKFC GCDNPFDKTI AQLSELYPEF
MSNFLQSSHF SSKTGLMKEI VVNSLDNLFK EHPYTKSIDA SYIYRVKEST TCYEDDWAKP
VYD
