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CDS information : Vanco_00020


close this sectionLocation

Organism
StrainATCC 19795 (=NBRC 12806)
Entry nameVancomycin
Contig
Start / Stop / Direction1,208 / 2,248 / + [in whole cluster]
1,208 / 2,248 / + [in contig]
Location1208..2248 [in whole cluster]
1208..2248 [in contig]
TypeCDS
Length1,041 bp (346 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category4.4 resistance
Productputative D-alanine--D-lactate ligase
Product (GenBank)D-alanine-D-alanine ligase
Gene
Gene (GenBank)vanA
EC number6.1.2.1
Keyword
Note
  • The N-terminal position was modified from original INSDC entry.
Note (GenBank)
Reference
ACC
Related Reference
ACC
Q9S611
PmId
[9791137] DdlN from vancomycin-producing Amycolatopsis orientalis C329.2 is a VanA homologue with D-alanyl-D-lactate ligase activity. (J Bacteriol. , 1998)
ACC
O33806
NITE
A4793_00320
PmId
[9177243] D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are highly homologous to the enterococcal vancomycin-resistance ligases VanA and VanB. (Proc Natl Acad Sci U S A. , 1997)
[12060705] Assembling the glycopeptide antibiotic scaffold: The biosynthesis of A47934 from Streptomyces toyocaensis NRRL15009. (Proc Natl Acad Sci U S A. , 2002)
ACC
Q06893
PmId
[7957913] Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583. (FEBS Lett. , 1994)
ACC
P25051
PmId
[1998664] Identification of vancomycin resistance protein VanA as a D-alanine:D-alanine ligase of altered substrate specificity. (Biochemistry. , 1991)
[1931965] Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. (Biochemistry. , 1991)
[1522072] The cytoplasmic peptidoglycan precursor of vancomycin-resistant Enterococcus faecalis terminates in lactate. (J Bacteriol. , 1992)
[10908650] The molecular basis of vancomycin resistance in clinically relevant Enterococci: crystal structure of D-alanyl-D-lactate ligase (VanA). (Proc Natl Acad Sci U S A. , 2000)
ACC
R4SMX3
PmId
[24884615] Complete genome sequence and comparative genomic analyses of the vancomycin-producing Amycolatopsis orientalis. (BMC Genomics. , 2014)

close this sectionSequence

selected fasta
>putative D-alanine--D-lactate ligase [D-alanine-D-alanine ligase]
MGRLKLGIIFGGTGEEHPISVKSAREVANSLDIEKYEPYYIGITLNGEWKLCDGPSADWE
SGNCRPVIVSPDRSAHGLLVLDEGKYETIALDVVLPVLHGKFGEDGAMQGLLELSGIPYV
GCDVQSSALCMDKSLTYTVVRSAGIATPNFWIVTADNDVDPDELTYPVFVKPARSGSSFG
VSKVTSKEELAAALETAREFDSKVLIEETVIGSEIGCSILGNDGDLLAGEVDRVALTHGF
FKIHQEESPETGSENSTFIVPADIPAESRTLVQETAKVIYRTLGCRGLARVDLFLKEDGS
VVLNEVNTLPGLTSYSRYPRMMAAAGIPLGDLIDRLVTLTLAGRNG
selected fasta
>putative D-alanine--D-lactate ligase [D-alanine-D-alanine ligase]
ATGGGTAGGTTGAAACTCGGCATCATCTTCGGGGGAACTGGCGAAGAGCACCCTATCTCC
GTCAAATCCGCGCGTGAGGTGGCGAACAGCCTCGACATCGAAAAGTACGAGCCGTACTAC
ATCGGTATCACCCTGAACGGCGAATGGAAGCTCTGCGACGGCCCGAGCGCGGACTGGGAG
TCCGGCAACTGCCGCCCCGTCATCGTGTCGCCGGACCGGAGCGCGCACGGCCTGCTGGTC
CTCGACGAGGGCAAGTACGAAACGATCGCCCTCGACGTGGTGCTGCCGGTCCTGCACGGC
AAGTTCGGCGAAGACGGCGCGATGCAGGGCCTGCTGGAACTCTCCGGCATCCCCTACGTG
GGCTGCGACGTCCAGAGCTCCGCCCTGTGCATGGACAAGTCCCTCACCTACACCGTCGTC
CGGAGCGCGGGCATCGCCACGCCGAACTTCTGGATCGTCACCGCGGACAACGACGTCGAT
CCCGACGAGCTCACCTACCCCGTCTTCGTGAAGCCGGCCCGTTCCGGTTCGTCCTTCGGT
GTCAGCAAGGTGACCAGCAAGGAAGAACTGGCGGCGGCACTGGAAACCGCGCGCGAGTTC
GACTCGAAGGTGCTGATCGAAGAAACCGTCATCGGCAGTGAGATCGGCTGCTCCATCCTG
GGCAACGACGGGGATCTGCTGGCCGGCGAGGTGGACCGCGTCGCGCTGACCCACGGCTTC
TTCAAGATCCACCAGGAAGAGAGCCCTGAGACCGGCTCCGAGAACTCGACGTTCATCGTG
CCCGCCGACATCCCGGCGGAGTCGCGCACGCTCGTCCAGGAGACGGCGAAGGTCATCTAC
CGCACCCTGGGCTGCCGGGGCCTCGCGCGCGTGGACCTCTTCCTCAAGGAAGACGGCAGC
GTCGTGCTCAACGAGGTCAACACCCTGCCCGGCCTGACCTCGTACAGCCGTTACCCGCGG
ATGATGGCCGCCGCCGGTATCCCGCTCGGCGACTTGATCGACCGGCTGGTGACGTTGACC
TTGGCGGGCCGTAACGGATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR000291 D-alanine--D-alanine ligase/VANA/B/C, conserved site (Conserved_site)
 [99-110]  PS00843
PS00843   DALA_DALA_LIGASE_1
 [283-311]  PS00844
PS00844   DALA_DALA_LIGASE_2
IPR005905 D-alanine--D-alanine ligase (Family)
 [4-341]  35.872 MF_00047
MF_00047   Dala_Dala_lig
 [5-340]  1.3e-85 TIGR01205
TIGR01205   D_ala_D_alaTIGR: D-alanine--D-alanine ligase
IPR011095 D-alanine--D-alanine ligase, C-terminal (Domain)
 [140-337]  1e-68 PF07478
PF07478   Dala_Dala_lig_C
IPR011127 D-alanine--D-alanine ligase, N-terminal (Domain)
 [5-122]  8.3e-30 PF01820
PF01820   Dala_Dala_lig_N
IPR011761 ATP-grasp fold (Domain)
 [137-338]  49.852 PS50975
PS50975   ATP_GRASP
IPR013815 ATP-grasp fold, subdomain 1 (Domain)
 [136-210]  1.1e-25 G3DSA:3.30.1490.20
G3DSA:3.30.1490.20   no description
IPR013816 ATP-grasp fold, subdomain 2 (Domain)
 [211-339]  1.2e-35 G3DSA:3.30.470.20
G3DSA:3.30.470.20   no description
IPR016185 Pre-ATP-grasp fold (Domain)
 [2-131]  4.9e-38 SSF52440
SSF52440   PreATP-grasp domain
 [3-121]  6.6e-32 G3DSA:3.40.50.20
G3DSA:3.40.50.20   no description
SignalP No significant hit
TMHMM No significant hit