SELO_SHESW
ID SELO_SHESW Reviewed; 484 AA.
AC A1RPL0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
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};
GN OrderedLocusNames=Sputw3181_3800;
OS Shewanella sp. (strain W3-18-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=351745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W3-18-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. W3-18-1.";
RL Submitted (DEC-2006) 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; CP000503; ABM26605.1; -; Genomic_DNA.
DR RefSeq; WP_011791032.1; NC_008750.1.
DR AlphaFoldDB; A1RPL0; -.
DR SMR; A1RPL0; -.
DR KEGG; shw:Sputw3181_3800; -.
DR HOGENOM; CLU_010245_4_1_6; -.
DR OMA; YGPYGWL; -.
DR Proteomes; UP000002597; 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..484
FT /note="Protein adenylyltransferase SelO"
FT /id="PRO_1000045261"
FT ACT_SITE 244
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 81..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 115..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
SQ SEQUENCE 484 AA; 54587 MW; 3134A2158EFF1A5F CRC64;
MQFKQDFFTQ LPEFYSQVYP QGLSHPQWLA WSHDAAQLIG LTQPTDELLL GLSGNAAIDG
ATYYAQVYSG HQFGGYTPRL GDGRSIILGE AIGPNGAWDV ALKGGGPTPY SRHGDGRAVM
RSAVREFLVS EALYHLHVPT TRALAVIGSD MPVWRESQET AAITVRLARS HIRFGHFEFF
CHSERGRADK LLQLLNFTIT QHYPHLSCDP SGYKAWFLQV VQDTAKMIAH WQAVGFAHGV
MNTDNMSILG DSFDFGPFAF LDTFQEDFIC NHSDPEGRYA FGQQPGVGLW NLQRLAQALT
PVIPSDDLIA ILNQYQEALV QTYLLLMRAK LGLTTLDKST AEQDKQDLEL IGQFTVLMEK
NQLDYAQTWR QFGQLDPRSQ HSSLRDDFID THQFDTWYKA YQLRLGDVTD IAAWQTERNS
VNPKYILRNY LAQEAIIAVE EGNLAPLQRL QQVLSRPFAE QVEHDELAKR PPDWGQGLIM
SCSS
