ID   MAV_MYCA1               Reviewed;         825 AA.
AC   A0QLI5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Putative NAD(+)--arginine ADP-ribosyltransferase Mav;
DE            EC=2.4.2.31;
DE   AltName: Full=Putative mono(ADP-ribosyl)transferase;
DE            Short=mADPRT;
DE            Short=mART;
DE   AltName: Full=Toxin Mav;
GN   OrderedLocusNames=MAV_4644;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUGGESTION OF FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=104;
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).
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}. Note=May be secreted by
CC       the ESX (type VII) secretion system. {ECO:0000269|PubMed:21170356}.
CC   -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000479; ABK66967.1; -; Genomic_DNA.
DR   RefSeq; WP_011726171.1; NC_008595.1.
DR   AlphaFoldDB; A0QLI5; -.
DR   SMR; A0QLI5; -.
DR   EnsemblBacteria; ABK66967; ABK66967; MAV_4644.
DR   KEGG; mav:MAV_4644; -.
DR   HOGENOM; CLU_013587_1_0_11; -.
DR   OMA; RNGLCSI; -.
DR   OrthoDB; 1019126at2; -.
DR   Proteomes; UP000001574; 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   GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR   InterPro; IPR000768; ART.
DR   Pfam; PF01129; ART; 1.
DR   PROSITE; PS51996; TR_MART; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; NAD; NADP; Nucleotide-binding; Nucleotidyltransferase;
KW   Secreted; Toxin; Transferase; Virulence.
FT   CHAIN           1..825
FT                   /note="Putative NAD(+)--arginine ADP-ribosyltransferase
FT                   Mav"
FT                   /id="PRO_0000410946"
FT   DOMAIN          650..825
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   REGION          435..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..564
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..593
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        730
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        755
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        795
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   BINDING         687..699
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         730..733
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         750
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         795
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   825 AA;  83406 MW;  88923E4692849614 CRC64;
     MAPLACDPTA LDHAGATVVA AGESLGSVIS TLTAALAGTS GMAGDDPVGA ALGRRYDGAA
     AKLIQAMADT RNGLCSIGDG VRMSAHNYAV AEAMSDLAGR ASALPAPQVT GPLTVGAPPS
     AVGHGSGAPA GWGWVAPSIG MIWPTGDSAK LRAAAAAWAT AGANFMAAET AAGGGTMAAI
     GAQQIPEGAA INKALADASS ATADVARQCQ TIAAQLNSYA AKVDQVHAAI LDLLSRICDP
     LTGIKEVWDL LTDEDEDEIK KIADDIRTVV DNFGREADTL GGQIEATVSA VAAATENMSH
     WAGKEWDHFL HGTPVGRALN QVGQAFKGVG EEGWGFLKGL YEVSPNRMLL DPVGYGKTMA
     GMVEGAGTLV GLGPDGVPGA FDAWKALGKD VTHWDEWGSN PAEALGKSTF DVATLALPGG
     PLSKLGKFGH SAADALKGLK KPPGVPKPPE VKPPAAPKAP DSGQPAPSGK PGPVAPSGKP
     APGPADGPLP HSPTESKPPA GGTPPAAEPP KPTAAPHSGE PKPIATPPES VGKPVTPAPA
     EGAPAQPHEP VSARVPPTVP AADTPAPSAP AASMSAASGP PMPPTPSLPE PASLPSGPSG
     DLPAETPPTA GIPHSGEPSA PSSVPPHFPD TPTHGLGDGG AHGPPESDPK NANGHGPHDA
     SLDSGSDHHL PLHPLDSDDL AALAHYTGPG YQELNFALRE GALDVSQQAR VDALQKALEK
     LPVYEGAVVR GTNLPADVLE QYRPGEVITE AAFTSTSTDH TVAQSSAFAG NTEFRIWSTT
     GRDVSSVSMY PDEKEILFPA GSKFYVVSKT VDPQTGRTII EMIER