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Q1JL27 (DDL_STRPC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:MGAS9429_Spy1205
OrganismStreptococcus pyogenes serotype M12 (strain MGAS9429) [Complete proteome] [HAMAP]
Taxonomic identifier370551 [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_1000030501

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
Q1JL27 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: BC221F78EBD31314

FASTA34838,969
        10         20         30         40         50         60 
MSKQTLVLLY GGRSAEREVS VLSAESVMRA VNYDKFLVKT YFITQMGQFI KTQQFSEKPS 

        70         80         90        100        110        120 
ESERLMTNET IELTQKIKPS DIYEEGAVVF PVLHGPMGED GSIQGFLEVL RMPYIGTNVM 

       130        140        150        160        170        180 
SSSIAMDKIT TKRVLESIGI PQVAYTVYID GQDLEACLVE TLARLTFPIF VKPANMGSSV 

       190        200        210        220        230        240 
GISKAQTKVE LRKAIQLALT YDSRVLIEQG VVAREIEVGL LGNDKVKSTL PGEVIKDVDF 

       250        260        270        280        290        300 
YDYQAKYVDN KITMAIPADV DQSIVTEMRS YAEVAFKALG GCGLSRCDFF LTQDGQVYLN 

       310        320        330        340 
ELNTMPGFTQ WSMYPLLWEN MGLAYPDLIE ELVTLAQEMF DQRESHLI 

« Hide

References

[1]"Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus."
Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS9429.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000259 Genomic DNA. Translation: ABF32392.1.
RefSeqYP_596936.1. NC_008021.1.

3D structure databases

ProteinModelPortalQ1JL27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370551.MGAS9429_Spy1205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF32392; ABF32392; MGAS9429_Spy1205.
GeneID4061939.
KEGGspk:MGAS9429_Spy1205.
PATRIC19753463. VBIStrPyo37061_1221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSPYO370551:GHLY-1264-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_STRPC
AccessionPrimary (citable) accession number: Q1JL27
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 60 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