PHXA_PHOLL
ID PHXA_PHOLL Reviewed; 408 AA.
AC Q7N8B1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Photox toxin;
DE EC=2.4.2.31;
DE AltName: Full=Mono(ADP-ribosyl)transferase;
DE Short=mADPRT;
DE Short=mART;
DE AltName: Full=NAD(+)--arginine ADP-ribosyltransferase;
GN Name=phxA; OrderedLocusNames=plu0822;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
RN [2]
RP FUNCTION AS A TOXIN, ACTIN AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF ARG-288; 318-SER--SER-320; GLU-353 AND GLU-355, EXPRESSION
RP IN YEAST, AND LACK OF NAD(+)-GLYCOHYDROLASE ACTIVITY.
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=20181945; DOI=10.1074/jbc.m109.077339;
RA Visschedyk D.D., Perieteanu A.A., Turgeon Z.J., Fieldhouse R.J.,
RA Dawson J.F., Merrill A.R.;
RT "Photox, a novel actin-targeting mono-ADP-ribosyltransferase from
RT Photorhabdus luminescens.";
RL J. Biol. Chem. 285:13525-13534(2010).
CC -!- FUNCTION: Mono-ADP-ribosylates chicken skeletal alpha-actin and human
CC non-skeletal beta- and gamma-actin. Mono-ADP-ribosylates 'Arg-177' of
CC yeast actin, blocking its ability to polymerize. Does not possess
CC NAD(+)-glycohydrolase activity, unlike most mART enzymes. Upon
CC expression in S.cerevisiae almost completely inhibits growth.
CC {ECO:0000269|PubMed:20181945}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.4 uM for NAD(+) {ECO:0000269|PubMed:20181945};
CC KM=0.60 uM for alpha-actin {ECO:0000269|PubMed:20181945};
CC Note=Measured on chicken skeletal alpha-actin.;
CC -!- SIMILARITY: In the C-terminal section; belongs to the SpvB family.
CC {ECO:0000305}.
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DR EMBL; BX571861; CAE13117.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7N8B1; -.
DR SMR; Q7N8B1; -.
DR STRING; 243265.plu0822; -.
DR EnsemblBacteria; CAE13117; CAE13117; plu0822.
DR KEGG; plu:plu0822; -.
DR HOGENOM; CLU_674135_0_0_6; -.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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 Pfam; PF03496; ADPrib_exo_Tox; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; NAD; NADP; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Toxin; Transferase; Virulence.
FT CHAIN 1..408
FT /note="Photox toxin"
FT /id="PRO_0000410491"
FT DOMAIN 190..393
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT REGION 168..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT MUTAGEN 288
FT /note="R->A: 20000-fold reduction in mART activity. 4-fold
FT decrease in NAD(+) affinity."
FT /evidence="ECO:0000269|PubMed:20181945"
FT MUTAGEN 318..320
FT /note="STS->ATA: 2000-fold reduction in mART activity. 5-
FT fold decrease in NAD(+) affinity."
FT /evidence="ECO:0000269|PubMed:20181945"
FT MUTAGEN 353..355
FT /note="EAE->AAA: Total suppression of toxicity in yeast."
FT MUTAGEN 353
FT /note="E->A: 20% growth in yeast, 13000-fold reduction in
FT mART activity. No change in NAD(+) affinity."
FT /evidence="ECO:0000269|PubMed:20181945"
FT MUTAGEN 355
FT /note="E->A: 40% growth in yeast, 600-fold reduction in
FT mART activity. 4-fold decrease in NAD(+) affinity."
FT /evidence="ECO:0000269|PubMed:20181945"
SQ SEQUENCE 408 AA; 45857 MW; 0881A030B0ACA9D1 CRC64;
MEKIMPISPI SGHMPLSQIQ VPQHATTSPL LEQGNRLFEQ SVRRGPLHFQ SSSLKHLCAE
LRQLQNAPSS MQARRVQDAI QHWENHHPKE VMARSTRLAE LKQALAEQGT VGRTLQSKVM
ATGPQVILKQ PMPALPQSIA AQITKAQTGC TTTLVSSATA ELIKHNQNNQ QHIKDSDGRK
PVNNMPPPPP PPMADKTQKV KKWVVNTDSK QLQALRYYSA QGYNLINTYL RGGEYVKHQA
IETLLSRNYL HSNEPTPQEF DAGMRAYIQD VTEGLNELAI TDHKKVYRGL KFDKSELKNL
LDQYTTEGNI IAEKGFLSTS PDKAWVNDTI LVINLESGHK GRILGDAAHF KGEAEMLFPP
ESKMLVEKVL NRDDKEFDSH FSNLRLTDDA SADTTRIKRI INIKMLNE
