{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q88LS1","uniProtkbId":"EARP_PSEPK","entryAudit":{"firstPublicDate":"2021-06-02","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2003-06-01","entryVersion":94,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)","taxonId":160488,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein-arginine rhamnosyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"value":"2.4.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28951478"}],"value":"EF-P arginine rhamnosyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28951478"}],"value":"earP"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAN67476.1"}],"value":"PP_1857"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"value":"Protein-arginine rhamnosyltransferase that catalyzes the transfer of a single rhamnose to elongation factor P (EF-P) on 'Lys-32', a modification required for EF-P-dependent rescue of polyproline stalled ribosomes"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dTDP-beta-L-rhamnose + L-arginyl-[protein] = N(omega)-(alpha-L-rhamnosyl)-L-arginyl-[protein] + dTDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66692"},{"database":"Rhea","id":"RHEA-COMP:10532"},{"database":"Rhea","id":"RHEA-COMP:17096"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29965"},{"database":"ChEBI","id":"CHEBI:57510"},{"database":"ChEBI","id":"CHEBI:58369"},{"database":"ChEBI","id":"CHEBI:167445"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66693"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}]}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":53.0,"unit":"uM","substrate":"dTDP-beta-L-rhamnose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"value":"kcat is 35 min(-1) with dTDP-beta-L-rhamnose substrate."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"value":"Adopts a GT-B fold and acts as an inverting enzyme that converts the beta-configuration in the dTDP-beta-L-rhamnose donor to the alpha configuration in the N-linked (Rha) arginine product"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyltransferase 104 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"Protein-arginine rhamnosyltransferase","featureId":"PRO_0000452682"},{"type":"Active site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}]},{"type":"Active site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}]},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57510"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5NV8"}],"ligand":{"name":"dTDP-beta-L-rhamnose","id":"ChEBI:CHEBI:57510"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57510"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5NV8"}],"ligand":{"name":"dTDP-beta-L-rhamnose","id":"ChEBI:CHEBI:57510"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57510"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5NV8"}],"ligand":{"name":"dTDP-beta-L-rhamnose","id":"ChEBI:CHEBI:57510"}},{"type":"Binding site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57510"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5NV8"}],"ligand":{"name":"dTDP-beta-L-rhamnose","id":"ChEBI:CHEBI:57510"}},{"type":"Mutagenesis","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Abolished protein-arginine rhamnosyltransferase activity without affecting substrate-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Strongly reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"Abolished protein-arginine rhamnosyltransferase activity without affecting substrate-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["E","A"]}},{"type":"Mutagenesis","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"Reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"Reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"Reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"Strongly reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Strongly reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["D"]}},{"type":"Mutagenesis","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Abolished protein-arginine rhamnosyltransferase activity without affecting substrate-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q","A"]}},{"type":"Mutagenesis","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"Reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"Strongly reduced protein-arginine rhamnosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28951478"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":7,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Beta strand","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Turn","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Beta strand","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Beta strand","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Beta strand","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Beta strand","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Beta strand","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Beta strand","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Beta strand","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Turn","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]},{"type":"Helix","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5NV8"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"12534463","citationType":"journal article","authors":["Nelson K.E.","Weinel C.","Paulsen I.T.","Dodson R.J.","Hilbert H.","Martins dos Santos V.A.P.","Fouts D.E.","Gill S.R.","Pop M.","Holmes M.","Brinkac L.M.","Beanan M.J.","DeBoy R.T.","Daugherty S.C.","Kolonay J.F.","Madupu R.","Nelson W.C.","White O.","Peterson J.D.","Khouri H.M.","Hance I.","Chris Lee P.","Holtzapple E.K.","Scanlan D.","Tran K.","Moazzez A.","Utterback T.R.","Rizzo M.","Lee K.","Kosack D.","Moestl D.","Wedler H.","Lauber J.","Stjepandic D.","Hoheisel J.","Straetz M.","Heim S.","Kiewitz C.","Eisen J.A.","Timmis K.N.","Duesterhoeft A.","Tuemmler B.","Fraser C.M."],"citationCrossReferences":[{"database":"PubMed","id":"12534463"},{"database":"DOI","id":"10.1046/j.1462-2920.2002.00366.x"}],"title":"Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440.","publicationDate":"2002","journal":"Environ. Microbiol.","firstPage":"799","lastPage":"808","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"28951478","citationType":"journal article","authors":["Krafczyk R.","Macosek J.","Jagtap P.K.A.","Gast D.","Wunder S.","Mitra P.","Jha A.K.","Rohr J.","Hoffmann-Roder A.","Jung K.","Hennig J.","Lassak J."],"citationCrossReferences":[{"database":"PubMed","id":"28951478"},{"database":"DOI","id":"10.1128/mbio.01412-17"}],"title":"Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P.","publicationDate":"2017","journal":"MBio","firstPage":"0","lastPage":"0","volume":"8"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 2-377 IN COMPLEX WITH DTDP-BETA-L-RHAMNOSE","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","DOMAIN","ACTIVE SITES","MUTAGENESIS OF ASP-13; ASP-17; PHE-191; TYR-193; PHE-252; GLN-255; PHE-258; ARG-271; GLU-273; ASP-274; SER-275 AND TYR-291"],"referenceComments":[{"value":"ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"5NV8"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AE015451","properties":[{"key":"ProteinId","value":"AAN67476.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_010952888.1","properties":[{"key":"NucleotideSequenceId","value":"NC_002947.4"}]},{"database":"PDB","id":"5NV8","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.29 A"},{"key":"Chains","value":"A=2-377"}]},{"database":"PDBsum","id":"5NV8","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"Q88LS1","properties":[{"key":"Description","value":"-"}]},{"database":"BMRB","id":"Q88LS1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q88LS1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"160488.PP_1857","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GT104","properties":[{"key":"FamilyName","value":"Glycosyltransferase Family 104"}]},{"database":"PaxDb","id":"160488-PP_1857","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"83681607","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ppu:PP_1857","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|160488.4.peg.1958","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG4394","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_060250_0_0_6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"209085at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"Q88LS1","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"PPUT160488:G1G01-1961-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000556","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0106361","properties":[{"key":"GoTerm","value":"F:protein-arginine rhamnosyltransferase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"28951478"}]},{"database":"InterPro","id":"IPR016633","properties":[{"key":"EntryName","value":"EarP"}]},{"database":"NCBIfam","id":"TIGR03837","properties":[{"key":"EntryName","value":"efp_Arg_rhamno"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10093","properties":[{"key":"EntryName","value":"EarP"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF015557","properties":[{"key":"EntryName","value":"UCP015557"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKATWDIFCSVVDNYGDIGVTWRLARQLVAEHGLAVRLWVDDLNAFTPMCPGADATAAQQWQHGVDVRHWPAAWLPVAPADVVIGAFACQLPAAYVEAMRARPQPPLWLNLEYLSAEDWVEGCHGLPSPQPNGLRKVFFFPGFTDKTGGLLREGSLLARRDGFQQSAEARRAFLQGLGVDLVPGALLISLFAYENPQLGNWLDALATADQPCHLLVPQGRVVAGLSQWLGEGPLHVGDVRTRGALTVQVLPFVSQDDFDRLLWSCDFNAVRGEDSFVRAQWAGQPMLWHIYVQDENAHWEKLEAFLAHYRCGLSDDADAALLGLWRAWNMDFDMGQAWRAARQHWPELQQHARLWGARQAAQPDLATALVHFYRNSL","length":377,"molWeight":42150,"crc64":"CC3575AD1E26B155","md5":"203B366A6CDFEC8C72AC35B49C674767"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":4,"Mutagenesis":14,"Beta strand":9,"Helix":12,"Turn":2},"uniParcId":"UPI000000F093"}}