{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P77649","secondaryAccessions":["P76904"],"uniProtkbId":"SELO_ECOLI","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1997-02-01","entryVersion":140,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein nucleotidyltransferase SelO"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30270044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32966796"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35532215"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35532216"}],"value":"2.7.7.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30270044"}],"value":"Protein adenylyltransferase SelO"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30270044"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32966796"}],"value":"2.7.7.108"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein uridylyltransferase SelO"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32966796"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35532215"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35532216"}],"value":"2.7.7.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"30270044"}],"value":"Selenoprotein O homolog"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"30270044"}],"value":"SelO"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"30270044"}],"value":"selO"},"synonyms":[{"value":"ydiU"}],"orderedLocusNames":[{"value":"b1706"},{"value":"JW1696"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30270044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32966796"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35532215"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35532216"}],"value":"Nucleotidyltransferase involved in the post-translational modification of proteins (PubMed:30270044, PubMed:32966796, PubMed:35532215, PubMed:35532216). It can catalyze the addition of adenosine monophosphate (AMP) or uridine monophosphate (UMP) to a protein, resulting in modifications known as AMPylation and UMPylation (PubMed:30270044, PubMed:32966796, PubMed:35532215, PubMed:35532216). It could be involved in stress resistance and play a crucial role in regulating essential bacterial processes, including flagella synthesis and iron uptake (PubMed:32966796, PubMed:35532215, PubMed:35532216)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30270044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32966796"}],"value":"Can catalyze the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr and Tyr residues of target proteins (PubMed:30270044). In vitro, prefers ATP over other nucleotides as a cosubstrate (PubMed:30270044). Substrates include SelO itself, SucA, which is AMPylated on 'Thr-405', and GrxA, AMPylated on 'Tyr-13' (PubMed:30270044, PubMed:32966796). AMPylation of the grx family of enzymes may regulate protein S-glutathionylation levels in cells (PubMed:30270044). AMPylation is probably involved in redox homeostasis (PubMed:30270044)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32966796"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35532215"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35532216"}],"value":"Under stress conditions, may act primarily as an uridylyltransferase that catalyzes the UMPylation of various proteins, including chaperones and transcription factors such as FlhDC and Fur (PubMed:32966796, PubMed:35532215, PubMed:35532216). Can also catalyze auto-UMPylation (PubMed:32966796). It can catalyze the Mn(2+)-dependent UMPylation on Tyr and His residues of chaperones such as GroEL, DnaK, HtpG and ClpB, leading to their inactivation (PubMed:32966796). Catalyzes the UMPylation on Ser-31 of the FlhC subunit of the major flagellar transcriptional regulator complex FlhDC (PubMed:35532215). UMPylated FlhDC complex completely loses its DNA binding activity, which inhibits the expression of secondary and tertiary flagellar genes, and interrupts flagellar synthesis (PubMed:35532215). Also catalyzes the UMPylation on His-118 residue of the major iron uptake regulator Fur, which destroys Fur dimers, (PubMed:35532216). Fur loses its DNA binding activity and therefore its repressor activity, which induces the expression of genes involved in iron uptake (PubMed:35532216)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = 3-O-(5'-adenylyl)-L-seryl-[protein] + 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AMPylation activity is activated in reducing conditions (PubMed:30270044). Under non-reducing conditions, the formation of an intramolecular disulfide bond between Cys-272 and Cys-476 reduces the AMPylation activity (PubMed:30270044). Shows a preference for UTP over ATP in the presence of Mn(2+) (PubMed:32966796). The UMPylation activity depends on Mn(2+) (PubMed:32966796)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":1.9,"unit":"uM","substrate":"ATP","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30270044"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30270044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32966796"}],"value":"Auto-AMPylated (PubMed:30270044, PubMed:32966796). 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