SCARP_STRCO
ID SCARP_STRCO Reviewed; 204 AA.
AC Q9L1E4;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Guanine-specific ADP-ribosyl transferase {ECO:0000303|PubMed:23212047};
DE EC=2.4.2.- {ECO:0000269|PubMed:23212047, ECO:0000269|PubMed:30072382};
DE AltName: Full=NAD(+):guanine-N2-ADP-D-ribosyltransferase {ECO:0000303|PubMed:23212047};
DE AltName: Full=S.coelicolor ADP-ribosylating protein {ECO:0000303|PubMed:23212047};
DE Short=ScARP {ECO:0000303|PubMed:23212047};
DE Flags: Precursor;
GN OrderedLocusNames=SCO5461 {ECO:0000312|EMBL:CAB76015.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1] {ECO:0000312|EMBL:CAB76015.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLU-164.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=23212047; DOI=10.1016/j.toxicon.2012.11.019;
RA Nakano T., Matsushima-Hibiya Y., Yamamoto M., Takahashi-Nakaguchi A.,
RA Fukuda H., Ono M., Takamura-Enya T., Kinashi H., Totsuka Y.;
RT "ADP-ribosylation of guanosine by SCO5461 protein secreted from
RT Streptomyces coelicolor.";
RL Toxicon 63:55-63(2013).
RN [3] {ECO:0007744|PDB:5ZJ4, ECO:0007744|PDB:5ZJ5}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 43-204 WITH AND WITHOUT GDP AND
RP NADH, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, DOMAIN,
RP DISULFIDE BONDS, AND MUTAGENESIS OF TRP-159 AND GLN-162.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=30072382; DOI=10.1074/jbc.ac118.004412;
RA Yoshida T., Tsuge H.;
RT "Substrate N2 atom recognition mechanism in pierisin family DNA-targeting,
RT guanine-specific ADP-ribosyltransferase ScARP.";
RL J. Biol. Chem. 293:13768-13774(2018).
CC -!- FUNCTION: ADP-ribosylates the N2 amino group of guanosine,
CC deoxyguanosine, GMP, dGMP, cGMP, GTP and dGTP; oligo-guanosine, oligo-
CC deoxyguanosine and tRNA are ADP-ribosylated less efficiently, while
CC dsDNA is a very poor substrate (PubMed:23212047). Also acts on GDP
CC (PubMed:30072382). {ECO:0000269|PubMed:23212047,
CC ECO:0000269|PubMed:30072382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-guanosine +
CC nicotinamide; Xref=Rhea:RHEA:71643, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16750, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142714; Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyguanosine in DNA + NAD(+) = an N(2)-(ADP-L-ribosyl)-
CC 2'-deoxyguanosine in DNA + H(+) + nicotinamide; Xref=Rhea:RHEA:71807,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:18062, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:85445,
CC ChEBI:CHEBI:142722; Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-2'-
CC deoxyguanosine + nicotinamide; Xref=Rhea:RHEA:71879,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:142715;
CC Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GMP + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-GMP + nicotinamide;
CC Xref=Rhea:RHEA:71883, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:58115, ChEBI:CHEBI:142717;
CC Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-GTP + nicotinamide;
CC Xref=Rhea:RHEA:71887, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57540, ChEBI:CHEBI:142719;
CC Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGMP + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-dGMP +
CC nicotinamide; Xref=Rhea:RHEA:71891, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57673,
CC ChEBI:CHEBI:142718; Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dGTP + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-dGTP +
CC nicotinamide; Xref=Rhea:RHEA:71895, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:61429,
CC ChEBI:CHEBI:142720; Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-3',5'-
CC cyclic GMP + nicotinamide; Xref=Rhea:RHEA:71899, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:142721; Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanine + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-guanine +
CC nicotinamide; Xref=Rhea:RHEA:71903, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16235, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142716; Evidence={ECO:0000269|PubMed:23212047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-GDP + nicotinamide;
CC Xref=Rhea:RHEA:71907, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:58189, ChEBI:CHEBI:142713;
CC Evidence={ECO:0000269|PubMed:30072382};
CC -!- ACTIVITY REGULATION: Inhibited by NADH. {ECO:0000269|PubMed:30072382}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 uM for guanosine {ECO:0000269|PubMed:23212047};
CC KM=52 uM for deoxyguanosine {ECO:0000269|PubMed:23212047};
CC KM=174 uM for guanine {ECO:0000269|PubMed:23212047};
CC KM=110 uM for NAD(+) {ECO:0000269|PubMed:23212047};
CC Note=kcat is 325 sec(-1) for guanosine, 278 sec(-1) for
CC deoxyguanosine, 63 sec(-1) for guanine, 512 sec(-1) for dGMP, 460
CC sec(-1) for GTP, 379 sec(-1) for dGTP, 204 sec(-1) for GMP, 148 sec(-
CC 1) for cGMP, between 0.14 and 0.26 sec(-1) for oligo(G) oligo(dG) and
CC tRNA and 0.001 sec(-1) for dsDNA. {ECO:0000269|PubMed:23212047};
CC pH dependence:
CC Optimum pH is 6-7. {ECO:0000269|PubMed:23212047};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:23212047};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:30072382}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23212047}.
CC -!- DOMAIN: The PN loop (phosphate-nicotinamide, residues 132-136) moves
CC dramatically upon GDP-binding. {ECO:0000269|PubMed:30072382}.
CC -!- MISCELLANEOUS: As this is a secreted protein it will have to find its
CC substrates extracellularly, probably from surrounding dead or damaged
CC cells. As many bacteria use guanosine derivatives to respond to
CC environmental changes, this enzyme may disregulate these responses.
CC {ECO:0000305|PubMed:30072382}.
CC -!- SIMILARITY: Belongs to the pierisin ADP-ribosyltransferase family.
CC {ECO:0000305|PubMed:30072382}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL939123; CAB76015.1; -; Genomic_DNA.
DR RefSeq; NP_629598.1; NC_003888.3.
DR RefSeq; WP_011030264.1; NZ_VNID01000011.1.
DR PDB; 5ZJ4; X-ray; 1.50 A; A/B/C/D=43-204.
DR PDB; 5ZJ5; X-ray; 1.57 A; A/B=43-204.
DR PDBsum; 5ZJ4; -.
DR PDBsum; 5ZJ5; -.
DR SMR; Q9L1E4; -.
DR STRING; 100226.SCO5461; -.
DR GeneID; 1100901; -.
DR KEGG; sco:SCO5461; -.
DR PATRIC; fig|100226.15.peg.5545; -.
DR eggNOG; COG1396; Bacteria.
DR HOGENOM; CLU_097942_0_0_11; -.
DR InParanoid; Q9L1E4; -.
DR OMA; DVNKTIG; -.
DR Proteomes; UP000001973; Chromosome.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycosyltransferase; Nucleotidyltransferase;
KW Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..42
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23212047"
FT CHAIN 43..204
FT /note="Guanine-specific ADP-ribosyl transferase"
FT /evidence="ECO:0000255"
FT /id="PRO_5030176823"
FT MOTIF 132..136
FT /note="PN (phosphate-nicotinamide) loop"
FT /evidence="ECO:0000305|PubMed:30072382"
FT BINDING 81..85
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:30072382,
FT ECO:0007744|PDB:5ZJ5"
FT BINDING 98
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:30072382,
FT ECO:0007744|PDB:5ZJ5"
FT BINDING 111..114
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:30072382,
FT ECO:0007744|PDB:5ZJ5"
FT BINDING 132..134
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:30072382,
FT ECO:0007744|PDB:5ZJ5"
FT BINDING 159
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:30072382,
FT ECO:0007744|PDB:5ZJ5"
FT BINDING 162
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:30072382,
FT ECO:0007744|PDB:5ZJ5"
FT DISULFID 46..76
FT /evidence="ECO:0000269|PubMed:30072382,
FT ECO:0007744|PDB:5ZJ4, ECO:0007744|PDB:5ZJ5"
FT DISULFID 180..194
FT /evidence="ECO:0000269|PubMed:30072382,
FT ECO:0007744|PDB:5ZJ4, ECO:0007744|PDB:5ZJ5"
FT MUTAGEN 159
FT /note="W->A: No ADP-ribosylation of GDP."
FT /evidence="ECO:0000269|PubMed:30072382"
FT MUTAGEN 162
FT /note="Q->E,N,S: No ADP-ribosylation of GDP."
FT /evidence="ECO:0000269|PubMed:30072382"
FT MUTAGEN 164
FT /note="E->D: No ADP-ribosylation of guanosine."
FT /evidence="ECO:0000269|PubMed:23212047"
SQ SEQUENCE 204 AA; 22386 MW; 1C9AB255AEB83215 CRC64;
MITTSLRRRT AAAVLSLSAV LATTAATAPG AAPAPSAAPA KAAPACPQFD DRTKAAADRG
VDVDRITPEP VWRTTCGTLY RSDSRGPQVV FEEGFHAKDV QNGQYDVEKY VLVNQPSPYV
STSYDHDLYK TWYKSGYNYY VDAPGGIDVN KTIGDTHKWA DQVEVAFPGG IQRKYIIGVC
PVDRQTKTEI MSDCESNPHY QPWH
