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Q04RK6 (DDL_LEPBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:LBJ_1946
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length351 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 – 351351D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000030461

Regions

Domain135 – 343209ATP-grasp
Nucleotide binding167 – 22256ATP By similarity

Sites

Metal binding2981Magnesium or manganese 1 By similarity
Metal binding3101Magnesium or manganese 1 By similarity
Metal binding3101Magnesium or manganese 2 By similarity
Metal binding3121Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04RK6 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: B2AF0D10AF638C4A

FASTA35138,303
        10         20         30         40         50         60 
MAKIAVFFGG SSTEHSISIR TGCFICRTLH TMGHSVKPIL LTQDGGWVVP LQYRISIPYE 

        70         80         90        100        110        120 
AVNSSDLFEE EFQKTNGVSK MDFISNLDAD IVFLGLHGGK GEDGSIQGFL RVLGVPYTGS 

       130        140        150        160        170        180 
GVAASALAMD KTRANQIFLQ SGQKVAPFFE VEKLGYTNSP EETVIKLMSL GFPQFLKPVE 

       190        200        210        220        230        240 
GGSSVSTYKI TNQEQLSRQL ALIFESDSKV MSQSFLAGTE VSCGVLERYR NGKLERIALP 

       250        260        270        280        290        300 
ATEIVPGGEF FDFESKYKQG GSREITPARI SKQEMTRVQE LAIDAHTSLG CRGYSRSDFI 

       310        320        330        340        350 
IVGGEPHILE TNTLPGMTET SLIPQQAKAA GITMEEVFAD LIEIGLKHSI H 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000350 Genomic DNA. Translation: ABJ76464.1.
RefSeqYP_801222.1. NC_008510.1.

3D structure databases

ProteinModelPortalQ04RK6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355277.LBJ_1946.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ76464; ABJ76464; LBJ_1946.
GeneID4411465.
KEGGlbj:LBJ_1946.
PATRIC22359561. VBILepBor13265_2485.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011592.
KOK01921.
OMADRIQAND.
OrthoDBEOG6ND0KB.

Enzyme and pathway databases

BioCycLBOR355277:GHYM-1922-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_LEPBJ
AccessionPrimary (citable) accession number: Q04RK6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 59 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