SELO_PSESM
ID SELO_PSESM Reviewed; 487 AA.
AC Q87VB1;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein adenylyltransferase SelO {ECO:0000255|HAMAP-Rule:MF_00692, ECO:0000305|PubMed:30270044};
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P77649, ECO:0000255|HAMAP-Rule:MF_00692};
DE EC=2.7.7.n1 {ECO:0000250|UniProtKB:P77649, ECO:0000255|HAMAP-Rule:MF_00692};
GN Name=selO {ECO:0000255|HAMAP-Rule:MF_00692}; OrderedLocusNames=PSPTO_5028;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
RP MAGNESIUM, AND ACTIVE SITE.
RX PubMed=30270044; DOI=10.1016/j.cell.2018.08.046;
RA Sreelatha A., Yee S.S., Lopez V.A., Park B.C., Kinch L.N., Pilch S.,
RA Servage K.A., Zhang J., Jiou J., Karasiewicz-Urbanska M., Lobocka M.,
RA Grishin N.V., Orth K., Kucharczyk R., Pawlowski K., Tomchick D.R.,
RA Tagliabracci V.S.;
RT "Protein AMPylation by an Evolutionarily Conserved Pseudokinase.";
RL Cell 175:809-821(2018).
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, ECO:0000305|PubMed:30270044}.
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:0000250|UniProtKB:P77649, ECO:0000255|HAMAP-
CC Rule:MF_00692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54289;
CC Evidence={ECO:0000250|UniProtKB:P77649, ECO:0000255|HAMAP-
CC 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:0000250|UniProtKB:P77649, ECO:0000255|HAMAP-
CC Rule:MF_00692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54293;
CC Evidence={ECO:0000250|UniProtKB:P77649, ECO:0000255|HAMAP-
CC 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:0000250|UniProtKB:P77649,
CC ECO:0000255|HAMAP-Rule:MF_00692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58121;
CC Evidence={ECO:0000250|UniProtKB:P77649, ECO:0000255|HAMAP-
CC Rule:MF_00692};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00692,
CC ECO:0000269|PubMed:30270044};
CC -!- SIMILARITY: Belongs to the SELO family. {ECO:0000255|HAMAP-
CC Rule:MF_00692, ECO:0000305}.
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DR EMBL; AE016853; AAO58456.1; -; Genomic_DNA.
DR RefSeq; NP_794761.1; NC_004578.1.
DR RefSeq; WP_011105279.1; NC_004578.1.
DR PDB; 6EAC; X-ray; 2.27 A; A/B/C/D=1-487.
DR PDBsum; 6EAC; -.
DR AlphaFoldDB; Q87VB1; -.
DR SMR; Q87VB1; -.
DR STRING; 223283.PSPTO_5028; -.
DR EnsemblBacteria; AAO58456; AAO58456; PSPTO_5028.
DR GeneID; 1186713; -.
DR KEGG; pst:PSPTO_5028; -.
DR PATRIC; fig|223283.9.peg.5147; -.
DR eggNOG; COG0397; Bacteria.
DR HOGENOM; CLU_010245_4_1_6; -.
DR OMA; YGPYGWL; -.
DR OrthoDB; 130048at2; -.
DR PhylomeDB; Q87VB1; -.
DR Proteomes; UP000002515; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..487
FT /note="Protein adenylyltransferase SelO"
FT /id="PRO_0000121422"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000305|PubMed:30270044"
FT BINDING 90..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000269|PubMed:30270044, ECO:0007744|PDB:6EAC"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000269|PubMed:30270044, ECO:0007744|PDB:6EAC"
FT BINDING 125..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000269|PubMed:30270044, ECO:0007744|PDB:6EAC"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000269|PubMed:30270044, ECO:0007744|PDB:6EAC"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000269|PubMed:30270044, ECO:0007744|PDB:6EAC"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000269|PubMed:30270044, ECO:0007744|PDB:6EAC"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000269|PubMed:30270044, ECO:0007744|PDB:6EAC"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:6EAC"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:6EAC"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:6EAC"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 162..179
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:6EAC"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 220..242
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6EAC"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 292..306
FT /evidence="ECO:0007829|PDB:6EAC"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 323..338
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:6EAC"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 432..443
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 448..458
FT /evidence="ECO:0007829|PDB:6EAC"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:6EAC"
SQ SEQUENCE 487 AA; 55208 MW; 8339BA64BD094EB2 CRC64;
MKALDELVFD NRFARLGDAF STHVLPEPID APRLVVASES ALALLDLAPE QSELPLFAEI
FSGHKLWAEA EPRAMVYSGH QFGSYNPRLG DGRGLLLGEV YNDAGEHWDL HLKGAGRTPY
SRMGDGRAVL RSSIREFLAS EALHALGIPS SRAACVVSSN TPVWREKQEY AAMVLRLAQS
HVRFGSLEYL FYTKQPEHLK TLAEHVLTMH YPHCQEQPEP YLAMFREIVE RNAELIAKWQ
AYGFCHGVMN TDNMSILGIT FDFGPFAFLD DFDEHFICNH SDHEGRYSFS NQVPIAQWNL
SALGQALTPF VSVEALRETI GLFLPLYQAH YLDLMRRRLG LTVAQDQDDK LVSQLLQLMQ
NSGVDYTLFF RRLGDQPAAQ ALRALRDDFV DIKVFDDWAQ AYQARIAAEE NGTEQARKER
MHAVNPLYIL RNYLAQNAIE AAEKGDYEEV RRLHQVLCTP FTEQPGMEGY AQRPPDWGKH
LEISCSS
