SELO_CLOPE
ID SELO_CLOPE Reviewed; 490 AA.
AC Q06373;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 115.
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=CPE0035;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 3628 / NCIMB 10662 / Type C;
RX PubMed=8423073; DOI=10.1128/iai.61.2.457-463.1993;
RA Katayama S., Matsushita O., Minami J., Mizobuchi S., Okabe A.;
RT "Comparison of the alpha-toxin genes of Clostridium perfringens type A and
RT C strains: evidence for extragenic regulation of transcription.";
RL Infect. Immun. 61:457-463(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-332.
RC STRAIN=8-6 / Type A;
RX PubMed=2560137; DOI=10.1007/bf00259619;
RA Saint-Joanis B., Garnier T., Cole S.T.;
RT "Gene cloning shows the alpha-toxin of Clostridium perfringens to contain
RT both sphingomyelinase and lecithinase activities.";
RL Mol. Gen. Genet. 219:453-460(1989).
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, ECO:0000305}.
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DR EMBL; D10248; BAA01092.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB79741.1; -; Genomic_DNA.
DR EMBL; X17300; CAA35187.1; -; Genomic_DNA.
DR PIR; JQ0367; JQ0367.
DR RefSeq; WP_011009583.1; NC_003366.1.
DR AlphaFoldDB; Q06373; -.
DR SMR; Q06373; -.
DR STRING; 195102.gene:10489265; -.
DR EnsemblBacteria; BAB79741; BAB79741; BAB79741.
DR KEGG; cpe:CPE0035; -.
DR HOGENOM; CLU_010245_4_1_9; -.
DR OMA; YGPYGWL; -.
DR Proteomes; UP000000818; 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; Reference proteome; Transferase.
FT CHAIN 1..490
FT /note="Protein adenylyltransferase SelO"
FT /id="PRO_0000121413"
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"
FT VARIANT 48
FT /note="E -> K (in strain: 8-6)"
FT VARIANT 56
FT /note="V -> I (in strain: 8-6)"
FT VARIANT 76
FT /note="V -> T (in strain: 8-6)"
FT VARIANT 109
FT /note="C -> G (in strain: 8-6 and NCIB 10662)"
FT VARIANT 149
FT /note="G -> S (in strain: 8-6)"
FT VARIANT 171
FT /note="R -> K (in strain: 8-6)"
FT VARIANT 201
FT /note="E -> D (in strain: NCIB 10662)"
FT VARIANT 220..221
FT /note="DN -> KS (in strain: NCIB 10662)"
FT VARIANT 220
FT /note="D -> N (in strain: 8-6)"
FT VARIANT 332
FT /note="N -> S (in strain: 8-6)"
FT VARIANT 347
FT /note="T -> A (in strain: NCIB 10662)"
FT VARIANT 481
FT /note="D -> N (in strain: NCIB 10662)"
SQ SEQUENCE 490 AA; 55805 MW; 90195AD52364E51D CRC64;
MDNKNFQSKT GFNLENTYLT LPNIFFSEQN PKGSKNPKLI KFNTSLAEEL GLNEEVLNSD
FGLNIFAGNE TFPGIVPIAQ AYAGHQFGHF TMLGDGRALL LGEHVTKDCK RYDVQLKGSG
RTIYSRGGDG KAALAPMLRE YIISEGMHGL GIPTTRSLAV VSTGEEVLRE RFEQGAILTR
IASSHIRVGT FAYAAQWGTL EDLKSLADYT IKRHFPNIAD NENKYILFLE EVINRQAELI
VKWQSVGFIH GVMNTDNMVI SGETIDYGPC AFMDTYDTNT VFSSIDYAGR YAYGNQPNMA
LWNLARFSEA LLPLLNPNLD EAVNIAKKSI SNFSKLYKKY WFNKMRTKLG LFTEKENDEL
LIEGLLSTMQ KYEADFTNTF VSLTLNKFED EKVFSSDEFK TWYALWQNRL KEENRPQEEV
RNLMMNNNPY IIPRNHLVEE ALKNAEKGDF TFMDNLLEAL KNPYSYSKDL EKYTKLPEKS
DTPYVTYCGT
