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Q6WRY5

- Q6WRY5_ENTFL

UniProt

Q6WRY5 - Q6WRY5_ENTFL

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Protein

D-alanine--D-alanine ligase

Gene

vanG

Organism
Enterococcus faecalis (Streptococcus faecalis)
Status
Unreviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Cell wall formation.UniRule annotationSAAS annotation

Catalytic activityi

ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+SAAS annotation, Mn2+SAAS annotationNote: Binds 2 magnesium or manganese ions per subunit.SAAS annotation
  • Mg2+UniRule annotation, Mn2+UniRule annotationNote: Binds 2 magnesium or manganese ions per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei140 – 1401ADPCombined sources
Binding sitei190 – 1901ADPCombined sources
Binding sitei226 – 2261ADPCombined sources
Binding sitei261 – 2611ADPCombined sources
Metal bindingi299 – 2991Magnesium or manganese 1UniRule annotation
Binding sitei301 – 3011ADPCombined sources
Metal bindingi312 – 3121Magnesium or manganese 1UniRule annotation
Metal bindingi312 – 3121Magnesium or manganese 2UniRule annotation
Metal bindingi314 – 3141Magnesium or manganese 2UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 22856ATPUniRule annotationAdd
BLAST
Nucleotide bindingi181 – 1833ADPCombined sources
Nucleotide bindingi219 – 2224ADPCombined sources
Nucleotide bindingi311 – 3122ADPCombined sources

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. D-alanine-D-alanine ligase activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  3. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationSAAS annotation

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradationUniRule annotationSAAS annotation, Peptidoglycan synthesisUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, MagnesiumUniRule annotationSAAS annotation, ManganeseUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15480.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanine--D-alanine ligaseUniRule annotation (EC:6.3.2.4UniRule annotation)
Alternative name(s):
D-Ala-D-Ala ligaseUniRule annotation
D-alanylalanine synthetaseUniRule annotation
Gene namesi
Name:vanGImported
Synonyms:ddlUniRule annotation
OrganismiEnterococcus faecalis (Streptococcus faecalis)Imported
Taxonomic identifieri1351 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FU0X-ray2.35A/B1-349[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini144 – 345202ATP-graspUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the D-alanine--D-alanine ligase family.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation
Contains ATP-grasp domain.SAAS annotation

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
HAMAPiMF_00047. Dala_Dala_lig.
InterProiIPR011761. 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]
PANTHERiPTHR23132. PTHR23132. 1 hit.
PfamiPF07478. Dala_Dala_lig_C. 1 hit.
PF01820. Dala_Dala_lig_N. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00843. DALA_DALA_LIGASE_1. 1 hit.
PS00844. DALA_DALA_LIGASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6WRY5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQNKKIAVIF GGNSTEYEVS LQSASAVFEN INTNKFDIIP IGITRSGEWY
60 70 80 90 100
HYTGEKEKIL NNTWFEDSKN LCPVVVSQNR SVKGFLEIAS DKYRIIKVDL
110 120 130 140 150
VFPVLHGKNG EDGTLQGIFE LAGIPVVGCD TLSSALCMDK DRAHKLVSLA
160 170 180 190 200
GISVPKSVTF KRFNEEAAMK EIEANLTYPL FIKPVRAGSS FGITKVIEKQ
210 220 230 240 250
ELDAAIELAF EHDTEVIVEE TINGFEVGCA VLGIDELIVG RVDEIELSSG
260 270 280 290 300
FFDYTEKYTL KSSKIYMPAR IDAEAEKRIQ EAAVTIYKAL GCSGFSRVDM
310 320 330 340
FYTPSGEIVF NEVNTIPGFT SHSRYPNMMK GIGLSFSQML DKLIGLYVE
Length:349
Mass (Da):38,730
Last modified:July 5, 2004 - v1
Checksum:i458EABDDF90493FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY271782 Genomic DNA. Translation: AAQ16273.1.
DQ212986 Genomic DNA. Translation: ABA71731.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY271782 Genomic DNA. Translation: AAQ16273.1 .
DQ212986 Genomic DNA. Translation: ABA71731.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4FU0 X-ray 2.35 A/B 1-349 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00219 .
BioCyci MetaCyc:MONOMER-15480.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
HAMAPi MF_00047. Dala_Dala_lig.
InterProi IPR011761. 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 ]
PANTHERi PTHR23132. PTHR23132. 1 hit.
Pfami PF07478. Dala_Dala_lig_C. 1 hit.
PF01820. Dala_Dala_lig_N. 1 hit.
[Graphical view ]
SUPFAMi SSF52440. SSF52440. 1 hit.
TIGRFAMsi TIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS00843. DALA_DALA_LIGASE_1. 1 hit.
PS00844. DALA_DALA_LIGASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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: BM4518Imported.
  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: G1-01247Imported.
  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.

Entry informationi

Entry nameiQ6WRY5_ENTFL
AccessioniPrimary (citable) accession number: Q6WRY5
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 7, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.