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A5VIS1 (DDL_LACRD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-alanine--D-alanine ligase

EC=6.3.2.4
Alternative name(s):
D-Ala-D-Ala ligase
D-alanylalanine synthetase
Gene names
Name:ddl
Ordered Locus Names:Lreu_0477
OrganismLactobacillus reuteri (strain DSM 20016) [Complete proteome] [HAMAP]
Taxonomic identifier557436 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cell wall formation By similarity. HAMAP-Rule MF_00047

Catalytic activity

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

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00047

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00047.

Sequence similarities

Belongs to the D-alanine--D-alanine ligase family.

Contains 1 ATP-grasp domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_0000341122

Regions

Domain140 – 346207ATP-grasp
Nucleotide binding170 – 22556ATP By similarity

Sites

Metal binding3001Magnesium or manganese 1 By similarity
Metal binding3131Magnesium or manganese 1 By similarity
Metal binding3131Magnesium or manganese 2 By similarity
Metal binding3151Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VIS1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: D8E60A5F98B34B71

FASTA37842,511
        10         20         30         40         50         60 
MTQKLHIALL FGGNSSEHDV SKRSAHNIYD ALDKEKYDVS LFMFTKDGIL LGNEDSQKIF 

        70         80         90        100        110        120 
DGEPEDQVVA EAYQKMDMSS PLAPIMALNE QKEIDFFFPV IHGNLGEDGT IQGLFKLLNK 

       130        140        150        160        170        180 
PYVGSNIAAS AMSFDKDLTK KIISQAGIRN TPYVVVTPEN QADYSWGRIE EKLGNLTFVK 

       190        200        210        220        230        240 
PAKQGSSVGI HRVTNAEEYE KALDDAFKYD YKILVEQGIA NPQEIEISIL GNEHPIASKL 

       250        260        270        280        290        300 
GAVRVPKDDP FYDYENKFVD ASGVVFELPV KLPQYLVDEI TDMALKAYKA LGMKGMARID 

       310        320        330        340        350        360 
FLVDSNNVPY LGEPNTLPGF TNISLYPQMW EVSGISYSDL IDRLIQLGLQ EFERNSKIKY 

       370 
DFRKLGTERV GQKKYNED 

« Hide

References

[1]"The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri."
Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L. expand/collapse author list , Ivanova N., Kyrpides N.C., Walter J.
PLoS Genet. 7:E1001314-E1001314(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 20016.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000705 Genomic DNA. Translation: ABQ82745.1.
RefSeqYP_001271082.1. NC_009513.1.

3D structure databases

ProteinModelPortalA5VIS1.
SMRA5VIS1. Positions 4-358.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557436.Lreu_0477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ82745; ABQ82745; Lreu_0477.
GeneID5188977.
KEGGlre:Lreu_0477.
PATRIC22254071. VBILacReu87937_0492.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011593.
KOK01921.
OMAQIDVIFP.
OrthoDBEOG64BQ73.

Enzyme and pathway databases

BioCycLREU557436:GC7Y-495-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
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 nameDDL_LACRD
AccessionPrimary (citable) accession number: A5VIS1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 10, 2007
Last modified: May 14, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways