{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P76938","secondaryAccessions":["P76497"],"uniProtkbId":"EPMC_ECOLI","entryAudit":{"firstPublicDate":"1999-07-15","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"1999-07-15","entryVersion":137,"sequenceVersion":2},"annotationScore":4.0,"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","source":"PubMed","id":"22706199"}],"value":"Elongation factor P lysine hydroxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22706199"}],"value":"EF-P lysine hydroxylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22706199"}],"value":"1.14.13.-"}]},"alternativeNames":[{"fullName":{"value":"EF-P post-translational modification enzyme C"}}]},"genes":[{"geneName":{"value":"epmC"},"synonyms":[{"value":"yfcM"}],"orderedLocusNames":[{"value":"b2326"},{"value":"JW5381"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22706199"}],"value":"Is involved in the final hydroxylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-((3R)-3,6-diaminohexanoyl)-L-lysyl-[protein] + NADPH + O2 + H(+) = N(6)-((3R)-3,6-diaminohexanoyl)-5-hydroxy-L-lysyl-[protein] + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83439"},{"database":"Rhea","id":"RHEA-COMP:20131"},{"database":"Rhea","id":"RHEA-COMP:20132"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:156053"},{"database":"ChEBI","id":"CHEBI:156054"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22706199"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:83440"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22706199"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22706199"}],"value":"Hydroxylation activity is abolished by NADP and increased by NADPH"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22706199"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23239623"}],"value":"EF-P proteins in the mutant strain displays a modification of +128 Da, whereas a modification of +144 Da is observed in wild-type strains. Cells lack CadA activity (lysine decarboxylase)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the EpmC family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Elongation factor P lysine hydroxylase","featureId":"PRO_0000169196"}],"keywords":[{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"9205837","citationType":"journal article","authors":["Yamamoto Y.","Aiba H.","Baba T.","Hayashi K.","Inada T.","Isono K.","Itoh T.","Kimura S.","Kitagawa M.","Makino K.","Miki T.","Mitsuhashi N.","Mizobuchi K.","Mori H.","Nakade S.","Nakamura Y.","Nashimoto H.","Oshima T.","Oyama S.","Saito N.","Sampei G.","Satoh Y.","Sivasundaram S.","Tagami H.","Takahashi H.","Takeda J.","Takemoto K.","Uehara K.","Wada C.","Yamagata S.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"9205837"},{"database":"DOI","id":"10.1093/dnares/4.2.91"}],"title":"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.","publicationDate":"1997","journal":"DNA Res.","firstPage":"91","lastPage":"113","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. III","Bloch C.A.","Perna N.T.","Burland V.","Riley M.","Collado-Vides J.","Glasner J.D.","Rode C.K.","Mayhew G.F.","Gregor J.","Davis N.W.","Kirkpatrick H.A.","Goeden M.A.","Rose D.J.","Mau B.","Shao Y."],"citationCrossReferences":[{"database":"PubMed","id":"9278503"},{"database":"DOI","id":"10.1126/science.277.5331.1453"}],"title":"The complete genome sequence of Escherichia coli K-12.","publicationDate":"1997","journal":"Science","firstPage":"1453","lastPage":"1462","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"16738553","citationType":"journal article","authors":["Hayashi K.","Morooka N.","Yamamoto Y.","Fujita K.","Isono K.","Choi S.","Ohtsubo E.","Baba T.","Wanner B.L.","Mori H.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"16738553"},{"database":"DOI","id":"10.1038/msb4100049"}],"title":"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.","publicationDate":"2006","journal":"Mol. Syst. Biol.","firstPage":"E1","lastPage":"E5","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"22706199","citationType":"journal article","authors":["Peil L.","Starosta A.L.","Virumae K.","Atkinson G.C.","Tenson T.","Remme J.","Wilson D.N."],"citationCrossReferences":[{"database":"PubMed","id":"22706199"},{"database":"DOI","id":"10.1038/nchembio.1001"}],"title":"Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.","publicationDate":"2012","journal":"Nat. Chem. Biol.","firstPage":"695","lastPage":"697","volume":"8"},"referencePositions":["FUNCTION AS EF-P HYDROXYLASE","CATALYTIC ACTIVITY","ACTIVITY REGULATION","GENE NAME","PATHWAY","DISRUPTION PHENOTYPE"],"referenceComments":[{"value":"K12 / AT713","type":"STRAIN"},{"value":"K12 / BW25113","type":"STRAIN"},{"value":"K12 / MC4100 / ATCC 35695 / DSM 6574","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"23239623","citationType":"journal article","authors":["Ude S.","Lassak J.","Starosta A.L.","Kraxenberger T.","Wilson D.N.","Jung K."],"citationCrossReferences":[{"database":"PubMed","id":"23239623"},{"database":"DOI","id":"10.1126/science.1228985"}],"title":"Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches.","publicationDate":"2013","journal":"Science","firstPage":"82","lastPage":"85","volume":"339"},"referencePositions":["DISRUPTION PHENOTYPE"],"referenceComments":[{"value":"K12 / BW25113","type":"STRAIN"},{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC75386.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAA16182.2"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"D65005","properties":[{"key":"EntryName","value":"D65005"}]},{"database":"RefSeq","id":"NP_416829.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_001089222.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"AlphaFoldDB","id":"P76938","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P76938","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4260792","properties":[{"key":"Interactions","value":"8"}]},{"database":"BioGRID","id":"851148","properties":[{"key":"Interactions","value":"4"}]},{"database":"DIP","id":"DIP-11984N","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"P76938","properties":[{"key":"Number of interactors","value":"28"}]},{"database":"IntAct","id":"P76938","properties":[{"key":"Interactions","value":"5"}]},{"database":"STRING","id":"511145.b2326","properties":[{"key":"Description","value":"-"}]},{"database":"jPOST","id":"P76938","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b2326","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC75386","properties":[{"key":"ProteinId","value":"AAC75386"},{"key":"GeneId","value":"b2326"}]},{"database":"GeneID","id":"946807","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW5381","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b2326","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_12960","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|511145.12.peg.2422","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB3869","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG3101","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_097152_0_0_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P76938","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"TQSQFEV","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"5298591at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P76938","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:G7201-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:G7201-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:P76938","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25274739"}]},{"database":"GO","id":"GO:0004497","properties":[{"key":"GoTerm","value":"F:monooxygenase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22706199"}]},{"database":"GO","id":"GO:0016709","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22706199"}]},{"database":"GO","id":"GO:0043687","properties":[{"key":"GoTerm","value":"P:post-translational protein modification"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"22706199"}]},{"database":"InterPro","id":"IPR007411","properties":[{"key":"EntryName","value":"EpmC"}]},{"database":"Pfam","id":"PF04315","properties":[{"key":"EntryName","value":"EpmC"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNSTHHYEQLIEIFNSCFADDFNTRLIKGDDEPIYLPADAEVPYNRIVFAHGFYASAIHEISHWCIAGKARRELVDFGYWYCPDGRDAQTQSQFEDVEVKPQALDWLFCVAAGYPFNVSCDNLEGDFEPDRVVFQRRVHAQVMDYLTNGIPERPARFIKALQNYYHTPELTAEQFPWPEALN","length":182,"molWeight":21146,"crc64":"ADD70D0BE3E3198A","md5":"BC76AF2C847ECF8F8E2068C3C0635024"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI000013AE10"}}