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Q4L7W2 (DDL_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:SH0954
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length356 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 – 356356D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000030496

Regions

Domain134 – 339206ATP-grasp
Nucleotide binding167 – 22256ATP By similarity

Sites

Metal binding2931Magnesium or manganese 1 By similarity
Metal binding3061Magnesium or manganese 1 By similarity
Metal binding3061Magnesium or manganese 2 By similarity
Metal binding3081Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4L7W2 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 637B3E71F8941058

FASTA35640,221
        10         20         30         40         50         60 
MVKENICIVY GGKSAEHDVS KLTAQNVLNA IDKERYLVDI IYITNDGLWK KKENITEEIK 

        70         80         90        100        110        120 
EIESLNMTDI EAGEITILLK ESSNGKPYDA IFPLLHGPNG EDGTIQGLFE VLDLPYVGNG 

       130        140        150        160        170        180 
VLAASSSMDK LVMKQLFEHR GLPQLPYISF LRSEYEKYEG NIIKLVKDKL TYPVFVKPAN 

       190        200        210        220        230        240 
LGSSVGISKC NNEDELKSGI EEAFQFDRKL VIEQGINARE VEVAVLGNDY PETTWPGEVI 

       250        260        270        280        290        300 
KDVAFYDYKS KYKDGKISLQ IPAELDEEVQ MTLRNMALEA FKATDCSGLV RADFFVTEDN 

       310        320        330        340        350 
QIFINETNAM PGFTAFSMYP SLWENMGLSY SDLITKLIDL AKERHEDKKK NKYTID 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE04263.1.
RefSeqYP_252869.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L7W2.
SMRQ4L7W2. Positions 3-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH0954.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE04263; BAE04263; SH0954.
GeneID3482296.
KEGGsha:SH0954.
PATRIC19617949. VBIStaHae67511_0941.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011593.
KOK01921.
OMAQIDVIFP.
OrthoDBEOG64BQ73.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-965-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_STAHJ
AccessionPrimary (citable) accession number: Q4L7W2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 2, 2005
Last modified: May 14, 2014
This is version 69 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