ID   SELO_CLOBA              Reviewed;         491 AA.
AC   B2V536;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=CLH_1334;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
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; CP001078; ACD51278.1; -; Genomic_DNA.
DR   RefSeq; WP_012449672.1; NC_010723.1.
DR   AlphaFoldDB; B2V536; -.
DR   SMR; B2V536; -.
DR   KEGG; cbt:CLH_1334; -.
DR   HOGENOM; CLU_010245_4_1_9; -.
DR   OMA; YGPYGWL; -.
DR   OrthoDB; 130048at2; -.
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_1000132099"
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;  55457 MW;  99D9564C322B2C49 CRC64;
     MKNKEIIINN YLNLENNYIK LPKKLFSEQN PSEVPSTNLV VFNESLASDL GLSEEFLQSD
     DGINFLSGNK ILEDTIPIAQ AYAGHQFGHF TMLGDGRAIL LGELKSQNGE RFDIQLKGSG
     RTPYSRGGDG KATLGAMLRE YIISEGMHGL GIPTTRSLAV VSTGEDVIRE EILKGAVLTR
     IAKSHIRVGT FQFISNYGTI EELKALADYT LNRHLKKAEY EGNPYIYLLN EVIKSQAKLI
     SKWQLVGFVH GVMNTDNVTI SGETIDYGPC AFMDVYDPDT VFSSIDINGR YAYGNQPKIG
     VWNLARFAET LLPLLDEDLE SAVEIAQNSI SKYSDLYNKY WYTGMRAKLG IFNEKEEDKE
     LIQSLLTMMK RFKADYTNTF SNLTLGNLSD IDMFASKEFK MWYEVWKERL KSQNQSSEES
     KMLMEKSNPT IIPRNNRVEE ALVAAIKDSD YSVMQSLLDV LKNPYDYSSI NEYYSIVPKS
     TSCTYKTYCG T