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Q6WRY5 (Q6WRY5_ENTFL) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
D-alanine--D-alanine ligase HAMAP-Rule MF_00047

EC=6.3.2.4 HAMAP-Rule MF_00047
Alternative name(s):
D-Ala-D-Ala ligase HAMAP-Rule MF_00047
D-alanylalanine synthetase HAMAP-Rule MF_00047
Gene names
Name:vanG EMBL AAQ16273.1
Synonyms:ddl HAMAP-Rule MF_00047
OrganismEnterococcus faecalis (Streptococcus faecalis) EMBL AAQ16273.1
Taxonomic identifier1351 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell wall formation By similarity. SAAS SAAS011127 HAMAP-Rule MF_00047

Catalytic activity

ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. SAAS SAAS011127 HAMAP-Rule MF_00047

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity. SAAS SAAS011127 HAMAP-Rule MF_00047

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. SAAS SAAS011127 HAMAP-Rule MF_00047

Subcellular location

Cytoplasm By similarity SAAS SAAS011127 HAMAP-Rule MF_00047.

Sequence similarities

Belongs to the D-alanine--D-alanine ligase family. HAMAP-Rule MF_00047

Contains 1 ATP-grasp domain. HAMAP-Rule MF_00047

Contains ATP-grasp domain. SAAS SAAS011127

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain144 – 345202ATP-grasp By similarity HAMAP-Rule MF_00047
Nucleotide binding173 – 22856ATP By similarity HAMAP-Rule MF_00047
Nucleotide binding181 – 1833ADP PDB 4FU0
Nucleotide binding219 – 2224ADP PDB 4FU0
Nucleotide binding311 – 3122ADP PDB 4FU0
Region188 – 1892Sulfate 1 binding PDB 4FU0
Region188 – 1892Sulfate 2 binding PDB 4FU0
Region264 – 2663Sulfate 4 binding PDB 4FU0
Region303 – 3053Sulfate 3 binding PDB 4FU0

Sites

Metal binding2991Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047
Metal binding3121Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047
Metal binding3121Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047
Metal binding3141Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047
Binding site1401ADP PDB 4FU0
Binding site1901ADP PDB 4FU0
Binding site2121Sulfate 2 PDB 4FU0
Binding site2231Sulfate 3 PDB 4FU0
Binding site2261ADP PDB 4FU0
Binding site2611ADP PDB 4FU0
Binding site2701Sulfate 4 PDB 4FU0
Binding site2971Sulfate 5 PDB 4FU0
Binding site2971Sulfate 6 PDB 4FU0
Binding site3011ADP PDB 4FU0
Binding site3141Sulfate 5 PDB 4FU0
Binding site3181Sulfate 5; via amide nitrogen PDB 4FU0
Binding site3181Sulfate 6; via amide nitrogen PDB 4FU0
Binding site3241Sulfate 6; via amide nitrogen PDB 4FU0
Binding site3361Sulfate 7; via amide nitrogen PDB 4FU0
Binding site3361Sulfate 8; via amide nitrogen PDB 4FU0

Sequences

Sequence LengthMass (Da)Tools
Q6WRY5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 458EABDDF90493FD

FASTA34938,730
        10         20         30         40         50         60 
MQNKKIAVIF GGNSTEYEVS LQSASAVFEN INTNKFDIIP IGITRSGEWY HYTGEKEKIL 

        70         80         90        100        110        120 
NNTWFEDSKN LCPVVVSQNR SVKGFLEIAS DKYRIIKVDL VFPVLHGKNG EDGTLQGIFE 

       130        140        150        160        170        180 
LAGIPVVGCD TLSSALCMDK DRAHKLVSLA GISVPKSVTF KRFNEEAAMK EIEANLTYPL 

       190        200        210        220        230        240 
FIKPVRAGSS FGITKVIEKQ ELDAAIELAF EHDTEVIVEE TINGFEVGCA VLGIDELIVG 

       250        260        270        280        290        300 
RVDEIELSSG FFDYTEKYTL KSSKIYMPAR IDAEAEKRIQ EAAVTIYKAL GCSGFSRVDM 

       310        320        330        340 
FYTPSGEIVF NEVNTIPGFT SHSRYPNMMK GIGLSFSQML DKLIGLYVE 

« Hide

References

[1]"The vanG glycopeptide resistance operon from Enterococcus faecalis revisited."
Depardieu F., Bonora M.G., Reynolds P.E., Courvalin P.
Mol. Microbiol. 50:931-948(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BM4518 EMBL AAQ16273.1.
[2]"VanG-type vancomycin-resistant Enterococcus faecalis strains isolated in Canada."
Boyd D.A., Du T., Hizon R., Kaplen B., Murphy T., Tyler S., Brown S., Jamieson F., Weiss K., Mulvey M.R.
Antimicrob. Agents Chemother. 50:2217-2221(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: G1-01247 EMBL ABA71731.1.
[3]"Structural and functional characterization of VanG D-Ala:D-Ser ligase associated with vancomycin resistance in Enterococcus faecalis."
Meziane-Cherif D., Saul F.A., Haouz A., Courvalin P.
J. Biol. Chem. 287:37583-37592(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH ADP AND SULFATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY271782 Genomic DNA. Translation: AAQ16273.1.
DQ212986 Genomic DNA. Translation: ABA71731.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FU0X-ray2.35A/B1-349[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15480.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
HAMAPMF_00047. Dala_Dala_lig.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR000291. D-Ala_lig_Van_CS.
IPR005905. D_ala_D_ala.
IPR011095. Dala_Dala_lig_C.
IPR011127. Dala_Dala_lig_N.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PANTHERPTHR23132. PTHR23132. 1 hit.
PfamPF07478. Dala_Dala_lig_C. 1 hit.
PF01820. Dala_Dala_lig_N. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS00843. DALA_DALA_LIGASE_1. 1 hit.
PS00844. DALA_DALA_LIGASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ6WRY5_ENTFL
AccessionPrimary (citable) accession number: Q6WRY5
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: March 19, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)