ID   SELO_XANOM              Reviewed;         518 AA.
AC   Q2P2A9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Protein adenylyltransferase SelO {ECO:0000255|HAMAP-Rule:MF_00692};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00692};
DE            EC=2.7.7.n1 {ECO:0000255|HAMAP-Rule:MF_00692};
GN   Name=selO {ECO:0000255|HAMAP-Rule:MF_00692}; OrderedLocusNames=XOO2563;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
CC   -!- FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to
CC       Ser, Thr or Tyr residues of target proteins (AMPylation).
CC       {ECO:0000255|HAMAP-Rule:MF_00692}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54289;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC         [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54293;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein]
CC         + diphosphate; Xref=Rhea:RHEA:58120, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:15073, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:142516; Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58121;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00692};
CC   -!- SIMILARITY: Belongs to the SELO family. {ECO:0000255|HAMAP-
CC       Rule:MF_00692}.
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DR   EMBL; AP008229; BAE69318.1; -; Genomic_DNA.
DR   RefSeq; WP_011408741.1; NC_007705.1.
DR   AlphaFoldDB; Q2P2A9; -.
DR   SMR; Q2P2A9; -.
DR   KEGG; xom:XOO2563; -.
DR   HOGENOM; CLU_010245_4_0_6; -.
DR   OMA; YGPYGWL; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00692; SelO; 1.
DR   InterPro; IPR003846; SelO.
DR   PANTHER; PTHR32057; PTHR32057; 1.
DR   Pfam; PF02696; SelO; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..518
FT                   /note="Protein adenylyltransferase SelO"
FT                   /id="PRO_0000271882"
FT   ACT_SITE        270
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         100..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         135..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
SQ   SEQUENCE   518 AA;  57747 MW;  4987ACEADDE771E5 CRC64;
     MTQLHFDNRL RQQLPGYQEE GARRREVRAA WSAVMPTPVA APYLIAHSAE MAHVLGLDAS
     EVASAAFAQV FGGNALYPGM QPWAVNYGGH QFGHWAGQLG DGRAISLGEA IGIDGGRYEL
     QLKGAGPTPY SRGADGRAVL RSSIREFLCS ESMHHLGVPT TRALSLVGTG DAVVRDMFYD
     GRPQREPGAI VCRVAPSFIR FGNFELPSAR GDNALLRQWV DFTIARDFPE LVGTAEALYA
     DWFAQVCQRT AVMVAHWMRV GFVHGVMNTD NMSILGLTID YGPYGWVDDY DPDWTPNTTD
     AQGRRYRFGT QPQVAYWNLG RLAQAMAPLF ADQAPLQQGL NRFRDTYLAC DRRDTAAKLG
     LAECRDEDLE LIDALRALMR DAEMDMTLTF RGLIDLSPVH PDPAQLHDAF YDDHKRVASA
     SQLQEWLQRY AARLQQDALS PDERRALMRL ANPRYVLRNY LAQQAIDQAE QGDPSGVQEL
     LEVMRRPYDD QSGRAAFAAR RPEWARDRAG CSMLSCSS