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P29827 (CINA_STRGV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lantibiotic cinnamycin
Alternative name(s):
Lanthiopeptin
Lantibiotic Ro 09-0198
Gene names
Name:cinA
Synonyms:rocA
OrganismStreptoverticillium griseoverticillatum
Taxonomic identifier68215 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length78 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Post-translational modification

Maturation of lantibiotics involves the enzymic 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.

Sequence similarities

Belongs to the type B lantibiotic family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5959 Potential
PRO_0000017148
Peptide60 – 7819Lantibiotic cinnamycin Ref.2 Ref.3
PRO_0000017149

Amino acid modifications

Modified residue741(3R)-3-hydroxyaspartate
Cross-link60 ↔ 77Beta-methyllanthionine (Cys-Thr)
Cross-link63 ↔ 73Lanthionine (Ser-Cys)
Cross-link64 ↔ 70Beta-methyllanthionine (Cys-Thr)
Cross-link65 ↔ 78Lysinoalanine (Ser-Lys)

Secondary structure

... 78
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29827 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 0ACDAE6BA54E5E7A

FASTA788,205
        10         20         30         40         50         60 
MTASILQQSV VDADFRAALL ENPAAFGASA AALPTPVEAQ DQASLDFWTK DIAATEAFAC 

        70 
RQSCSFGPFT FVCDGNTK 

« Hide

References

[1]"Prepeptide sequence of cinnamycin (Ro 09-0198): the first structural gene of a duramycin-type lantibiotic."
Kaletta C., Entian K.-D., Jung G.
Eur. J. Biochem. 199:411-415(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MAR 164C-MY6.
[2]"Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin."
Fredenhagen A., Fendrich G., Marki F., Marki W., Gruner J., Raschdorf F., Peter H.H.
J. Antibiot. 43:1403-1412(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-78.
[3]"Lanthiopeptin, a new peptide antibiotic. Production, isolation and properties of lanthiopeptin."
Naruse N., Tenmyo O., Tomita K., Konishi M., Miyaki T., Kawaguchi H., Fukase K., Wakamiya T., Shiba T.
J. Antibiot. 42:837-845(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-78, HYDROXYLATION AT ASP-74.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58545 Genomic DNA. Translation: CAA41436.1.
PIREWSMCN. A45767.
EWSMYG. S17181.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DDENMR-A60-78[»]
ProteinModelPortalP29827.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameCINA_STRGV
AccessionPrimary (citable) accession number: P29827
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 3, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families