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SELO_VIBVU
ID   SELO_VIBVU              Reviewed;         490 AA.
AC   Q8DG12;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=VV1_0039;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016795; AAO08581.1; -; Genomic_DNA.
DR   RefSeq; WP_011078163.1; NC_004459.3.
DR   AlphaFoldDB; Q8DG12; -.
DR   SMR; Q8DG12; -.
DR   EnsemblBacteria; AAO08581; AAO08581; VV1_0039.
DR   KEGG; vvu:VV1_0039; -.
DR   HOGENOM; CLU_010245_4_0_6; -.
DR   OMA; YGPYGWL; -.
DR   Proteomes; UP000002275; Chromosome 1.
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..490
FT                   /note="Protein adenylyltransferase SelO"
FT                   /id="PRO_0000121436"
FT   ACT_SITE        251
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         89..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         124..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
SQ   SEQUENCE   490 AA;  55849 MW;  B41EA72E3A8B3078 CRC64;
     MSLWSSVKFA QRYAQLPKVF YRLVTPQPLD NNRWVIWNGE LAQGFALPKH ADDPQLLSVF
     SGAEPFSAFK PLAMKYAGHQ FGVYNPDLGD GRGLLLGEMQ NQQGQWFDIH LKGAGLTPFS
     RMGDGRAVLR STLREYLCSE AMAALGIETT RALGMMVSDT PVYREQVEQG ACLIRLAQTH
     IRFGHFEHFF YTEQYDELRL LADNVIEWYM PECTAHDKPY LAMFEQVVAR TATMIAQWQA
     VGFAHGVMNT DNMSILGQTF DYGPFGFLDD YEPGYICNHS DYQGRYAFDQ QPRVALWNLS
     ALAHALSPLI ERDDLELALA QYEPTLGKVF SQLMRQKLGL LSQQEGDSEL FNAMFALLAE
     NHTDYTRFFR TLSQLDREDE QTVIDLFIDR DAAHGWLSRY LERVAMEQTA SGEAKSAQQR
     CEQMRAVNPK YILRNYLAQQ AIDKAQQGDF SEVHTLAKLL KNPYDEQAEM EAYAHLPPEW
     GKKMVISCSS
 
 
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