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CDS information : A4092_00130


close this sectionLocation

Organism
StrainATCC 39727
Entry nameA40926
Contig
Start / Stop / Direction15,271 / 15,861 / + [in whole cluster]
15,271 / 15,861 / + [in contig]
Location15271..15861 [in whole cluster]
15271..15861 [in contig]
TypeCDS
Length591 bp (196 aa)
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close this sectionAnnotation

Category4.4 resistance
ProductD-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine dipeptidase
DD-carboxypeptidase/DD-dipeptidase
Product (GenBank)putative VanY-type carboxypeptidase
Genedbv7
vanYn
Gene (GenBank)dbv7
EC number3.4.13.22
3.4.16.4
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[12837387] The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by nonomuraea species. (Chem Biol. , 2003)
[17873036] Phosphate-controlled regulator for the biosynthesis of the dalbavancin precursor A40926. (J Bacteriol. , 2007)
[20308385] Novel mechanism of glycopeptide resistance in the A40926 producer Nonomuraea sp. ATCC 39727. (Antimicrob Agents Chemother. , 2010)
[22788848] Characterization of VanYn, a novel D,D-peptidase/D,D-carboxypeptidase involved in glycopeptide antibiotic resistance in Nonomuraea sp. ATCC 39727. (FEBS J. , 2012)
[23497129] Streptomyces spp. as efficient expression system for a D,D-peptidase/D,D-carboxypeptidase involved in glycopeptide antibiotic resistance. (BMC Biotechnol. , 2013)
[24957828] Relationship between glycopeptide production and resistance in the actinomycete Nonomuraea sp. ATCC 39727. (Antimicrob Agents Chemother. , 2014)

close this sectionSequence

selected fasta
>D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine dipeptidase [putative VanY-type carboxypeptidase]
MRRSEGDDEPRTLPPRARDRVYTAVTRVLAVLLLPVAFVRQPGRARELACGWALRMRFPA
EDLTGLTDGARAAFTAARAEALWRHGQLVGLTSGYRDPRVQQRMFEEEVRRSGSVAAARM
FVAPPAESNHVKGMALDVRPHEGARWLEAHGARYDLYRIYDNEWWHFEHRPECGGTPPRR
LPHPGAAWASRNGGRV
selected fasta
>D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine dipeptidase [putative VanY-type carboxypeptidase]
ATGAGGAGAAGCGAGGGTGACGACGAACCACGCACTCTCCCGCCTCGGGCCCGGGACCGG
GTGTACACCGCGGTCACGCGGGTGCTCGCCGTGCTCCTGCTGCCCGTGGCGTTCGTCCGT
CAGCCCGGCCGCGCCCGCGAGCTGGCCTGCGGCTGGGCGTTGAGGATGCGATTCCCGGCA
GAGGACCTCACCGGGCTCACCGACGGCGCCAGGGCGGCGTTCACCGCGGCGCGGGCCGAG
GCGCTGTGGCGTCACGGCCAGCTCGTCGGTCTCACTTCCGGATACCGCGATCCCCGGGTC
CAGCAGCGGATGTTCGAGGAGGAGGTGCGCCGCTCAGGGTCCGTGGCCGCCGCACGGATG
TTCGTGGCGCCGCCGGCCGAGTCCAACCACGTCAAGGGCATGGCGCTGGACGTACGCCCG
CACGAGGGCGCGCGCTGGCTGGAGGCGCACGGCGCCCGCTACGACCTCTACCGCATCTAC
GACAACGAGTGGTGGCACTTCGAACACCGCCCGGAGTGCGGTGGCACGCCACCACGGCGG
CTACCCCACCCAGGCGCGGCCTGGGCGAGCCGGAACGGGGGCCGGGTCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR003709 Peptidase M15B/M15C (Domain)
 [66-171]  3.1e-13 PF02557
PF02557   VanY
IPR009045 Hedgehog signalling/DD-peptidase zinc-binding domain (Domain)
 [79-184]  3.30000164480624e-07 SSF55166
SSF55166   Hedgehog_sig_N
SignalP No significant hit
TMHMM
 [21-39]  Transmembrane (i-o)
Transmembrane 1