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CDS information : Teicp_00060


close this sectionLocation

Organism
StrainDSM 43866 (=NBRC 13999)
Entry nameTeicoplanin
Contig
Start / Stop / Direction6,645 / 7,682 / + [in whole cluster]
6,645 / 7,682 / + [in contig]
Location6645..7682 [in whole cluster]
6645..7682 [in contig]
TypeCDS
Length1,038 bp (345 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category4.4 resistance
Productputative D-alanine--D-lactate ligase
Product (GenBank)ligase
GenevanA
Gene (GenBank)
EC number6.1.2.1
Keyword
Note
Note (GenBank)
  • ORF6
Reference
ACC
PmId
[15113000] Biosynthetic gene cluster of the glycopeptide antibiotic teicoplanin: characterization of two glycosyltransferases and the key acyltransferase. (Chem Biol. , 2004)
Related Reference
ACC
Q70B05
NITE
Teicp2_00120
PmId
[11386360] Teicoplanin biosynthesis genes in Actinoplanes teichomyceticus. (Antonie Van Leeuwenhoek. , 2000)
[14702401] Organization of the teicoplanin gene cluster in Actinoplanes teichomyceticus. (Microbiology. , 2004)
[15500981] Glycopeptide resistance determinants from the teicoplanin producer Actinoplanes teichomyceticus. (FEMS Microbiol Lett. , 2004)
[17220405] Resistance to glycopeptide antibiotics in the teicoplanin producer is mediated by van gene homologue expression directing the synthesis of a modified cell wall peptidoglycan. (Antimicrob Agents Chemother. , 2007)
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
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
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)

close this sectionSequence

selected fasta
>putative D-alanine--D-lactate ligase [ligase]
MGKLKIGIIFGGVSEEHPVSIKSAQEVAKSLDAEKYEPYWIGITKDGAWRLCDGPGADWE
ISSARPAMLSPDRNVHGLLVQEDGRYREIRLDVVLPVLHGKLGEDGAMQGLFELSGIPYV
GCDVQSSAVCMDKSLTYAVVSSAGIAAATFWVVTPDEAPDPAQLTYPVFVKPARSGSSFG
VTKVSTEQELKAALETAREFDSKVLIEEAVVGSEIGCAIMGNDPDLVAGEVDRVALSHGF
FRIHQESEPERGSENSTFICPADIPAEARSLVQETAKAIYRALGCRGIARVDMFLKEDGT
VVLNEVNTLPGLTSYSRYPRMMAAAGIPLSAVIDQIVSLALPGDI
selected fasta
>putative D-alanine--D-lactate ligase [ligase]
ATGGGTAAGTTGAAGATCGGCATCATCTTCGGCGGCGTCTCCGAAGAGCACCCCGTCTCG
ATCAAGTCCGCGCAGGAGGTCGCCAAGAGCCTGGACGCCGAGAAGTACGAGCCGTACTGG
ATCGGCATCACGAAGGACGGCGCCTGGCGGCTGTGCGACGGCCCGGGCGCGGACTGGGAG
ATCAGCAGCGCCCGGCCGGCCATGCTGTCGCCGGACCGCAACGTCCACGGGCTGCTGGTC
CAGGAGGACGGCCGGTACCGGGAGATCCGCCTGGACGTCGTGCTGCCGGTTCTGCACGGC
AAGCTGGGCGAGGACGGCGCGATGCAGGGCCTGTTCGAGCTGTCCGGCATCCCCTACGTC
GGCTGTGACGTGCAGAGCTCCGCGGTCTGCATGGACAAGTCGCTGACCTACGCCGTGGTC
AGCAGCGCGGGCATCGCCGCCGCGACGTTCTGGGTCGTCACGCCGGACGAGGCGCCGGAC
CCCGCGCAGCTCACCTACCCGGTCTTCGTGAAGCCGGCCCGCTCGGGCTCCTCCTTCGGC
GTCACCAAGGTGTCGACCGAGCAGGAGCTGAAGGCCGCGCTGGAGACCGCGCGGGAGTTC
GACTCGAAGGTGCTGATCGAAGAGGCCGTGGTCGGCAGCGAGATCGGTTGCGCCATCATG
GGCAACGACCCGGACCTGGTCGCCGGCGAGGTGGACCGGGTCGCCCTGTCCCACGGCTTC
TTCCGGATCCACCAGGAGAGCGAGCCGGAGCGCGGTTCCGAGAACTCGACCTTCATCTGT
CCCGCCGACATCCCGGCCGAGGCGCGCTCGCTGGTCCAGGAGACGGCGAAGGCCATCTAC
CGTGCTCTGGGATGCCGCGGGATCGCCCGGGTGGACATGTTCCTCAAGGAGGACGGAACA
GTTGTCCTCAACGAGGTCAACACCCTGCCCGGCCTGACCTCGTACAGCCGTTACCCGCGC
ATGATGGCGGCTGCCGGGATTCCGCTCTCCGCGGTGATCGACCAGATCGTGTCGCTGGCC
CTGCCGGGGGACATCTGA

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)
 [5-340]  1.20000000000001e-86 TIGR01205
TIGR01205   D_ala_D_alaTIGR
IPR011095 D-alanine--D-alanine ligase, C-terminal (Domain)
 [140-337]  1.9e-69 PF07478
PF07478   Dala_Dala_lig_C
IPR011127 D-alanine--D-alanine ligase, N-terminal (Domain)
 [5-122]  1.69999999999999e-32 PF01820
PF01820   Dala_Dala_lig_N
IPR011761 ATP-grasp fold (Domain)
 [137-338]  PS50975
PS50975   ATP_GRASP
IPR013815 ATP-grasp fold, subdomain 1 (Domain)
 [123-210]  6.79999999999998e-25 G3DSA:3.30.1490.20
G3DSA:3.30.1490.20   ATP_grasp_subdomain_1
IPR013816 ATP-grasp fold, subdomain 2 (Domain)
 [211-341]  2.59999999999998e-37 G3DSA:3.30.470.20
G3DSA:3.30.470.20   ATP_grasp_subdomain_2
IPR016185 Pre-ATP-grasp fold (Domain)
 [2-121]  3.09999999999998e-36 G3DSA:3.40.50.20
G3DSA:3.40.50.20   Pre-ATP_grasp
 [2-131]  6.29998179434732e-40 SSF52440
SSF52440   PreATP-grasp-like
SignalP No significant hit
TMHMM No significant hit