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C0MCV8 (DDL_STRS7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:SZO_13560
OrganismStreptococcus equi subsp. zooepidemicus (strain H70) [Complete proteome] [HAMAP]
Taxonomic identifier553483 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length348 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 – 348348D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000202206

Regions

Domain132 – 334203ATP-grasp
Nucleotide binding162 – 21756ATP By similarity

Sites

Metal binding2881Magnesium or manganese 1 By similarity
Metal binding3011Magnesium or manganese 1 By similarity
Metal binding3011Magnesium or manganese 2 By similarity
Metal binding3031Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
C0MCV8 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 46FFE280C461ABA1

FASTA34838,931
        10         20         30         40         50         60 
MSKQTLILLY GGRSAEREVS VLSAESVMRA VDYTKFFVKT YFISQTGQFI KTQEFSSRPT 

        70         80         90        100        110        120 
LTERLMTNDT IRLEQQIRPS DIYEEGAVVF PVLHGPMGED GSIQGFLEVL RMPYVGTNIL 

       130        140        150        160        170        180 
SSSVAMDKIT TKRVLESAGI PQVAYTVYIE GQDLDRCLAE TEAALSYPVF VKPANMGSSV 

       190        200        210        220        230        240 
GISKAESEEE LRAAILLALT YDSRILIEQG VLAREIEVGL LGNTDVKSTL PGEVVKNVDF 

       250        260        270        280        290        300 
YDYQAKYIDN EITMAIPATI DESAMTSMRI YAETAFKAIG ACGLSRCDFF LGQDGQIYLN 

       310        320        330        340 
ELNTMPGFTQ WSMYPLLWEH MGLNYAELIE ELVRLAQEMF EKREGHLI 

« Hide

References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM204884 Genomic DNA. Translation: CAW99921.1.
RefSeqYP_002744870.1. NC_012470.1.

3D structure databases

ProteinModelPortalC0MCV8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING553483.SZO_13560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW99921; CAW99921; SZO_13560.
GeneID7694739.
KEGGseq:SZO_13560.
PATRIC19652486. VBIStrEqu35012_1439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011593.
KOK01921.
OMAMDKIAMK.
OrthoDBEOG64BQ73.
ProtClustDBPRK01966.

Enzyme and pathway databases

BioCycSEQU40041:GC8B-1449-MONOMER.
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 nameDDL_STRS7
AccessionPrimary (citable) accession number: C0MCV8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 38 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