SELO_BURPS
ID SELO_BURPS Reviewed; 521 AA.
AC Q63V22;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=BPSL1422;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH35424.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX571965; CAH35424.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004538218.1; NZ_CP009538.1.
DR RefSeq; YP_108044.1; NC_006350.1.
DR AlphaFoldDB; Q63V22; -.
DR SMR; Q63V22; -.
DR STRING; 272560.BPSL1422; -.
DR PRIDE; Q63V22; -.
DR EnsemblBacteria; CAH35424; CAH35424; BPSL1422.
DR KEGG; bps:BPSL1422; -.
DR PATRIC; fig|272560.51.peg.3441; -.
DR eggNOG; COG0397; Bacteria.
DR OMA; YGPYGWL; -.
DR Proteomes; UP000000605; 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; Reference proteome; Transferase.
FT CHAIN 1..521
FT /note="Protein adenylyltransferase SelO"
FT /id="PRO_0000271813"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 109..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 143..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692"
SQ SEQUENCE 521 AA; 57660 MW; 1F3D2AF5792F5CA1 CRC64;
MSFSRSEAAP AAPLPDLAAT LAAPRDDAFQ QLGAAFVTRL PAAPLPAPYV VGFSDDAARM
LGLEPALRDA PGFAELFCGN PTRDWPQASL PYASVYSGHQ FGVWAGQLGD GRALTIGELA
HDGRRYELQL KGAGRTPYSR MGDGRAVLRS SIREFLCSEA MHHLGIPTTR ALAVIGSDQP
VVREEIETSA VVTRVAQSFV RFGHFEHFFA NDRPEQLRAL ADHVIERFYP ACRDADDPYL
ALLAEATRRT AELVAQWQAV GFCHGVMNTD NMSILGLTID YGPFGFIDAF DAKHVCNHSD
TQGRYAYRMQ PRIAHWNCFC LAQALLPLIG LHRDAPSEDA RAERAVEDAH AVLGRFPEQF
GPALERAMRA KLGLALEREG DAALANQLLE IMDASHADFT LTFRHLARVS KHDARGDAPV
RDLFIDRDAF DRWANLYRAR LSEEARDDAS RAAAMNRVNP KYVLRNHLAE TAIRRAKEKD
FSEVERLAAV LRRPFDEQPE HDAYAALPPD WASTLEVSCS S
