SELO_ECOLI
ID SELO_ECOLI Reviewed; 478 AA.
AC P77649; P76904;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein adenylyltransferase SelO {ECO:0000255|HAMAP-Rule:MF_00692, ECO:0000305|PubMed:30270044};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00692, ECO:0000269|PubMed:30270044};
DE EC=2.7.7.n1 {ECO:0000255|HAMAP-Rule:MF_00692, ECO:0000269|PubMed:30270044};
DE AltName: Full=Selenoprotein O homolog {ECO:0000303|PubMed:30270044};
DE Short=SelO {ECO:0000303|PubMed:30270044};
GN Name=selO {ECO:0000255|HAMAP-Rule:MF_00692, ECO:0000303|PubMed:30270044};
GN Synonyms=ydiU; OrderedLocusNames=b1706, JW1696;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE, DISULFIDE BOND,
RP ACTIVE SITE, AND MUTAGENESIS OF LYS-107; GLU-130; ARG-170; ARG-177;
RP ASP-246; ASN-247; ASP-256; CYS-272 AND CYS-476.
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 and Tyr residues of target proteins (AMPylation). Cannot use
CC GTP, CTP or UTP as cosubstrate. AMPylates SucA at 'Thr-405' and GrxA on
CC 'Tyr-13'. Regulates protein S-glutathionylation levels probably by
CC AMPylation of deglutathionylation enzymes such as GrxA. Probably
CC involved in redox homeostasis. {ECO:0000269|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:0000255|HAMAP-Rule:MF_00692,
CC ECO:0000269|PubMed:30270044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54289;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00692,
CC ECO:0000269|PubMed:30270044};
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 ECO:0000269|PubMed:30270044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54293;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00692,
CC ECO:0000269|PubMed:30270044};
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 ECO:0000269|PubMed:30270044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58121;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00692,
CC ECO:0000269|PubMed:30270044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q87VB1,
CC ECO:0000255|HAMAP-Rule:MF_00692};
CC -!- ACTIVITY REGULATION: Activated in reducing conditions.
CC {ECO:0000269|PubMed:30270044}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for ATP {ECO:0000269|PubMed:30270044};
CC -!- PTM: Reduction/oxidation of the intramolecular disulfide bond involving
CC Cys-272 and Cys-476 regulates YdiU catalytic activity.
CC {ECO:0000269|PubMed:30270044}.
CC -!- DISRUPTION PHENOTYPE: Moderate decrease in global protein S-
CC glutathionylation. {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; U00096; AAC74776.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15475.1; -; Genomic_DNA.
DR PIR; B64929; B64929.
DR RefSeq; NP_416221.1; NC_000913.3.
DR RefSeq; WP_000175703.1; NZ_SSZK01000001.1.
DR PDB; 6III; X-ray; 2.11 A; A=1-474.
DR PDB; 6K20; X-ray; 2.58 A; A=1-478.
DR PDB; 6LNA; X-ray; 1.70 A; A/B=1-478.
DR PDBsum; 6III; -.
DR PDBsum; 6K20; -.
DR PDBsum; 6LNA; -.
DR AlphaFoldDB; P77649; -.
DR SMR; P77649; -.
DR BioGRID; 4260298; 13.
DR BioGRID; 850579; 4.
DR DIP; DIP-11762N; -.
DR IntAct; P77649; 7.
DR STRING; 511145.b1706; -.
DR jPOST; P77649; -.
DR PaxDb; P77649; -.
DR PRIDE; P77649; -.
DR EnsemblBacteria; AAC74776; AAC74776; b1706.
DR EnsemblBacteria; BAA15475; BAA15475; BAA15475.
DR GeneID; 946219; -.
DR KEGG; ecj:JW1696; -.
DR KEGG; eco:b1706; -.
DR PATRIC; fig|511145.12.peg.1777; -.
DR EchoBASE; EB3737; -.
DR eggNOG; COG0397; Bacteria.
DR HOGENOM; CLU_010245_4_1_6; -.
DR InParanoid; P77649; -.
DR OMA; YGPYGWL; -.
DR PhylomeDB; P77649; -.
DR BioCyc; EcoCyc:G6924-MON; -.
DR BioCyc; MetaCyc:G6924-MON; -.
DR PRO; PR:P77649; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
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; Disulfide bond; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..478
FT /note="Protein adenylyltransferase SelO"
FT /id="PRO_0000121416"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000305|PubMed:30270044"
FT BINDING 84..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1, ECO:0000255|HAMAP-
FT Rule:MF_00692"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1, ECO:0000255|HAMAP-
FT Rule:MF_00692"
FT BINDING 119..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1, ECO:0000255|HAMAP-
FT Rule:MF_00692"
FT BINDING 170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1, ECO:0000255|HAMAP-
FT Rule:MF_00692"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q87VB1, ECO:0000255|HAMAP-
FT Rule:MF_00692"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000305|PubMed:30270044"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00692,
FT ECO:0000305|PubMed:30270044"
FT DISULFID 272..476
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 107
FT /note="K->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 130
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 170
FT /note="R->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 177
FT /note="R->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 246
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 247
FT /note="N->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 256
FT /note="D->A: Loss of catalytic activity. Loss of ATP
FT binding."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 272
FT /note="C->A: Abolishes formation of the disulfide bond."
FT /evidence="ECO:0000269|PubMed:30270044"
FT MUTAGEN 476
FT /note="C->A: Abolishes formation of the disulfide bond."
FT /evidence="ECO:0000269|PubMed:30270044"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6K20"
FT HELIX 8..12
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6K20"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6LNA"
FT STRAND 156..173
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 214..236
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:6LNA"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 307..333
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 386..401
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 425..436
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:6LNA"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:6LNA"
SQ SEQUENCE 478 AA; 54382 MW; 02B392373872C584 CRC64;
MTLSFVTRWR DELPETYTAL SPTPLNNARL IWHNTELANT LSIPSSLFKN GAGVWGGEAL
LPGMSPLAQV YSGHQFGVWA GQLGDGRGIL LGEQLLADGT TMDWHLKGAG LTPYSRMGDG
RAVLRSTIRE SLASEAMHYL GIPTTRALSI VTSDSPVYRE TAEPGAMLMR VAPSHLRFGH
FEHFYYRRES EKVRQLADFA IRHYWSHLAD DEDKYRLWFS DVVARTASLI AQWQTVGFAH
GVMNTDNMSL LGLTLDYGPF GFLDDYEPGF ICNHSDHQGR YSFDNQPAVA LWNLQRLAQT
LSPFVAVDAL NEALDSYQQV LLTHYGERMR QKLGFMTEQK EDNALLNELF SLMARERSDY
TRTFRMLSLT EQHSAASPLR DEFIDRAAFD DWFARYRGRL QQDEVSDSER QQLMQSVNPA
LVLRNWLAQR AIEAAEKGDM TELHRLHEAL RNPFSDRDDD YVSRPPDWGK RLEVSCSS
