{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P29827","uniProtkbId":"CINA_STRGV","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1993-04-01","entryVersion":75,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces griseoverticillatus","commonName":"Streptoverticillium griseoverticillatum","taxonId":68215,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces","Streptomyces cinnamoneus group"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Lantibiotic cinnamycin"}},"alternativeNames":[{"fullName":{"value":"Lanthiopeptin"}},{"fullName":{"value":"Lantibiotic Ro 09-0198"}}],"flag":"Precursor"},"genes":[{"geneName":{"value":"cinA"},"synonyms":[{"value":"rocA"}]}],"comments":[{"texts":[{"value":"Can act as inhibitor of the enzyme phospholipase A2, and of the angiotensin-converting enzyme. Shows inhibitory activities against herpes simplex virus and immunopotentiating activities. Its antimicrobial activities are not very pronounced"}],"commentType":"FUNCTION"},{"texts":[{"value":"Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the type B lantibiotic family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Propeptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":"PRO_0000017148"},{"type":"Peptide","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Lantibiotic cinnamycin","featureId":"PRO_0000017149"},{"type":"Modified residue","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"(3R)-3-hydroxyaspartate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2544544"}]},{"type":"Cross-link","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Beta-methyllanthionine (Cys-Thr)"},{"type":"Cross-link","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Lanthionine (Ser-Cys)"},{"type":"Cross-link","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Beta-methyllanthionine (Cys-Thr)"},{"type":"Cross-link","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Lysinoalanine (Ser-Lys)"},{"type":"Beta strand","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2DDE"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0044","category":"Molecular function","name":"Antibiotic"},{"id":"KW-0929","category":"Molecular function","name":"Antimicrobial"},{"id":"KW-0078","category":"Molecular function","name":"Bacteriocin"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0379","category":"PTM","name":"Hydroxylation"},{"id":"KW-0425","category":"Molecular function","name":"Lantibiotic"},{"id":"KW-0883","category":"PTM","name":"Thioether bond"}],"references":[{"referenceNumber":1,"citation":{"id":"2070795","citationType":"journal article","authors":["Kaletta C.","Entian K.-D.","Jung G."],"citationCrossReferences":[{"database":"PubMed","id":"2070795"},{"database":"DOI","id":"10.1111/j.1432-1033.1991.tb16138.x"}],"title":"Prepeptide sequence of cinnamycin (Ro 09-0198): the first structural gene of a duramycin-type lantibiotic.","publicationDate":"1991","journal":"Eur. J. Biochem.","firstPage":"411","lastPage":"415","volume":"199"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"MAR 164C-MY6","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"2125590","citationType":"journal article","authors":["Fredenhagen A.","Fendrich G.","Marki F.","Marki W.","Gruner J.","Raschdorf F.","Peter H.H."],"citationCrossReferences":[{"database":"PubMed","id":"2125590"},{"database":"DOI","id":"10.7164/antibiotics.43.1403"}],"title":"Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin.","publicationDate":"1990","journal":"J. Antibiot.","firstPage":"1403","lastPage":"1412","volume":"43"},"referencePositions":["PROTEIN SEQUENCE OF 60-78"]},{"referenceNumber":3,"citation":{"id":"2544544","citationType":"journal article","authors":["Naruse N.","Tenmyo O.","Tomita K.","Konishi M.","Miyaki T.","Kawaguchi H.","Fukase K.","Wakamiya T.","Shiba T."],"citationCrossReferences":[{"database":"PubMed","id":"2544544"},{"database":"DOI","id":"10.7164/antibiotics.42.837"}],"title":"Lanthiopeptin, a new peptide antibiotic. Production, isolation and properties of lanthiopeptin.","publicationDate":"1989","journal":"J. Antibiot.","firstPage":"837","lastPage":"845","volume":"42"},"referencePositions":["PROTEIN SEQUENCE OF 60-78","HYDROXYLATION AT ASP-74"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X58545","properties":[{"key":"ProteinId","value":"CAA41436.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A45767","properties":[{"key":"EntryName","value":"EWSMCN"}]},{"database":"PIR","id":"S17181","properties":[{"key":"EntryName","value":"EWSMYG"}]},{"database":"PDB","id":"2DDE","properties":[{"key":"Method","value":"NMR"},{"key":"Resolution","value":"-"},{"key":"Chains","value":"A=60-78"}]},{"database":"PDBsum","id":"2DDE","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P29827","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P29827","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB04731","properties":[{"key":"GenericName","value":"1-ACETYL-2-LYSO-SN-GLYCERO-3-PHOSPHOETHANOLAMINE"}]},{"database":"InterPro","id":"IPR048275","properties":[{"key":"EntryName","value":"Cinnamycin_RiPP"}]},{"database":"InterPro","id":"IPR046016","properties":[{"key":"EntryName","value":"Dur/DurB-like"}]},{"database":"NCBIfam","id":"NF033431","properties":[{"key":"EntryName","value":"cinnamycin_RiPP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19398","properties":[{"key":"EntryName","value":"DurB-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTASILQQSVVDADFRAALLENPAAFGASAAALPTPVEAQDQASLDFWTKDIAATEAFACRQSCSFGPFTFVCDGNTK","length":78,"molWeight":8205,"crc64":"0ACDAE6BA54E5E7A","md5":"5ED65F2BCF6F97A9793A4AB43935E787"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Propeptide":1,"Peptide":1,"Modified residue":1,"Cross-link":4,"Beta strand":1},"uniParcId":"UPI000000D539"}}