ID   SELO_CLOB6              Reviewed;         491 AA.
AC   C3KTA3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
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=CLJ_B1236;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL   Submitted (MAY-2008) 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; CP001083; ACQ52289.1; -; Genomic_DNA.
DR   RefSeq; WP_003361155.1; NC_012658.1.
DR   AlphaFoldDB; C3KTA3; -.
DR   SMR; C3KTA3; -.
DR   EnsemblBacteria; ACQ52289; ACQ52289; CLJ_B1236.
DR   KEGG; cbi:CLJ_B1236; -.
DR   HOGENOM; CLU_010245_4_1_9; -.
DR   OMA; YGPYGWL; -.
DR   Proteomes; UP000002333; Chromosome.
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..491
FT                   /note="Protein adenylyltransferase SelO"
FT                   /id="PRO_1000212588"
FT   ACT_SITE        256
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         94..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         129..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
SQ   SEQUENCE   491 AA;  55346 MW;  AF6B05D0C42E3EE2 CRC64;
     MKERKVIIKT GLNLENSYTS LPEIFFTRQS PSRVPSPKLA VLNYPLITSL GLNAQVLQSA
     DGVDILAGNK IPEEAIPIAQ AYAGHQFAHF TMLGDGRALL LGEHITPLGD RFDIQLKGSG
     KTPYSRGGDG KAALGPMLRE YIISEAMNAL GIPTTRSLAV VTTGELIMRE AELPGAILTR
     VAASHIRVGT FEYVSRWGTV EELRALADYT LQRHFKKGYD KENPYLFLLQ EVIKKQAELI
     AKWQLVGFVH GVMNTDNMTI SGETIDYGPC AFMDVYNPKT VFSSIDIYGR YAYGNQPNIA
     AWNLARLAET LLPLLNINPN EAIKIAENAV SDFTKLYKNN WLSGMRAKLG IFNEEFQDEY
     LIEDLLSIMH KYGADYTNTF RALTFDNIED TVLFDKMEFD KWYKLWQERL TRQEESKLSS
     KQLMKSSNPS VIPRNHRVEE ALEAAVKEGD YSVMEKLLEA LSKPYAYSKE QDYYSKLPEP
     STCPYQTYCG T