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CDS information : Teicp2_00110


close this sectionLocation

Organism
StrainATCC 31121 (=NBRC 13999)
Entry nameTeicoplanin
Contig
Start / Stop / Direction12,219 / 13,259 / + [in whole cluster]
12,219 / 13,259 / + [in contig]
Location12219..13259 [in whole cluster]
12219..13259 [in contig]
TypeCDS
Length1,041 bp (346 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category4.4 resistance
Productputative D-lactate dehydrogenase
Product (GenBank)VanH protein
Genetcp2
vanHat
Gene (GenBank)tcp2
EC number
Keyword
Note
  • The N-terminal position was modified from original INSDC entry.
Note (GenBank)
Reference
ACC
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)
Related Reference
ACC
Q6ZZK3
NITE
Teicp_00050
PmId
[15113000] Biosynthetic gene cluster of the glycopeptide antibiotic teicoplanin: characterization of two glycosyltransferases and the key acyltransferase. (Chem Biol. , 2004)
ACC
O33805
NITE
A4793_00310
PmId
[10387095] Molecular mechanism of VanHst, an alpha-ketoacid dehydrogenase required for glycopeptide antibiotic resistance from a glycopeptide producing organism. (Biochemistry. , 1999)
ACC
Q05709
PmId
[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)
[1503450] Evidence for in vivo incorporation of D-lactate into peptidoglycan precursors of vancomycin-resistant enterococci. (Antimicrob Agents Chemother. , 1992)
[9605319] A thioredoxin fusion protein of VanH, a D-lactate dehydrogenase from Enterococcus faecium: cloning, expression, purification, kinetic analysis, and crystallization. (Protein Sci. , 1998)

close this sectionSequence

selected fasta
>putative D-lactate dehydrogenase [VanH protein]
MGYSEPVRAAAPRTRSLASSSSPVVPATGITIYGCGPDEAALFRELAPRFGVLPIITEAA
VSEANVNLASGNRCISVGHKTQITNGTLLALSRSGVKYISTRSIGYNHIDVAYAQSVGIS
VGNVAYSPDSVADYTLMLMLMAVRHMKAMIRRADVHDYRLNDVRGKELRDLTVGVVGTGR
IGSAVMDRLWGFGCRVLAYDNRRSDSAHYVPLDDLVRQSDIVTLHTPLTAATHHLLNQDR
IAQMRNGAFVINTGRGSLIDTEALVAALESDKLGGAALDVLEGEEGVFYADCRNKLIESK
ALLRLQEMPNVIISPHMAYYTDHALSDTVENSLVNCMNFEREQQHG
selected fasta
>putative D-lactate dehydrogenase [VanH protein]
ATGGGTTACAGCGAACCAGTACGAGCAGCGGCCCCCCGCACCCGATCGCTGGCCTCGTCG
TCCTCCCCGGTCGTTCCGGCAACGGGGATCACGATCTATGGATGCGGCCCGGATGAGGCC
GCCCTGTTCCGTGAGCTGGCGCCTCGCTTCGGCGTACTGCCGATCATCACGGAAGCGGCG
GTATCCGAGGCCAATGTGAATCTGGCATCCGGAAATCGATGCATCAGCGTCGGGCATAAG
ACTCAGATCACGAATGGCACGCTTCTCGCGCTGAGCCGATCCGGTGTGAAATACATCTCT
ACGCGGAGCATAGGCTACAACCACATCGATGTGGCGTATGCGCAGAGCGTGGGTATCTCC
GTCGGCAACGTCGCCTACTCGCCGGACAGCGTGGCCGATTACACGCTGATGCTGATGCTG
ATGGCCGTACGCCATATGAAAGCCATGATCCGCCGCGCGGACGTTCACGATTATCGATTG
AACGACGTGCGCGGGAAGGAACTGCGCGATCTGACCGTCGGGGTGGTCGGGACGGGGCGT
ATCGGTTCGGCCGTCATGGACCGGCTGTGGGGTTTCGGCTGCCGTGTGCTCGCCTACGAC
AATCGACGTTCGGATTCCGCTCATTATGTTCCGCTCGATGATTTGGTGCGGCAGAGCGAC
ATCGTCACACTTCACACCCCGCTCACCGCGGCCACGCACCATCTTCTCAACCAGGACCGT
ATCGCGCAGATGAGGAACGGTGCGTTCGTCATCAACACCGGGCGCGGTTCGCTTATCGAC
ACCGAGGCCCTCGTCGCAGCGCTGGAAAGCGACAAACTGGGTGGCGCGGCGCTCGATGTC
CTGGAAGGGGAGGAGGGGGTATTCTATGCCGACTGCCGTAACAAGCTCATTGAGAGCAAG
GCGCTGTTACGGCTACAGGAAATGCCCAATGTGATCATCAGCCCGCACATGGCCTACTAC
ACGGACCATGCGCTCAGCGACACTGTCGAGAACAGTCTCGTCAACTGCATGAACTTCGAG
AGGGAACAACAGCATGGGTAA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006139 D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain (Domain)
 [38-343]  5.5e-18 PF00389
PF00389   2-Hacid_dh
IPR006140 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding (Domain)
 [244-260]  PS00671
PS00671   D_2_HYDROXYACID_DH_3
 [173-200]  PS00065
PS00065   D_2_HYDROXYACID_DH_1
 [136-318]  1.2e-54 PF02826
PF02826   2-Hacid_dh_C
 [215-237]  PS00670
PS00670   D_2_HYDROXYACID_DH_2
IPR016040 NAD(P)-binding domain (Domain)
 [30-143]  5.30000000000001e-26 G3DSA:3.40.50.720 [144-318]  6e-60 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
SignalP No significant hit
TMHMM No significant hit