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Q5HUZ4 (DDL_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:CJE0889
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length346 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 – 346346D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000074768

Regions

Domain133 – 327195ATP-grasp
Nucleotide binding159 – 21153ATP By similarity

Sites

Metal binding2841Magnesium or manganese 1 By similarity
Metal binding2961Magnesium or manganese 1 By similarity
Metal binding2961Magnesium or manganese 2 By similarity
Metal binding2981Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HUZ4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: CDFAF5AB2726749A

FASTA34639,800
        10         20         30         40         50         60 
MKFAILFGGN SYEHEISIVS AVVLKKVINQ NLEFIFCDEE RRFYHIPSEK MNSKTFSTKA 

        70         80         90        100        110        120 
YKKEKELFIK QGGFFSKGFL KENKLECECV INLIHGRDGE DGKIAALFEF YSIKFIGPRL 

       130        140        150        160        170        180 
EASVLSFNKE LTKLYAKSVG VKTLDYTMVR KGQNSKEKLS FPCIIKPARL GSSIGISIVK 

       190        200        210        220        230        240 
DEKDLEYAKD VGFEFDNDLV VEEFKNNIKE YNLAGCMIND EFVFSIIEEP KKKEFLDFEQ 

       250        260        270        280        290        300 
KYLSFSGHNE LIEANLSEEL KEKLKDSFKK IYNPLFKGAL IRCDFFILDN EIYLNEINPN 

       310        320        330        340 
PGSLANYLFK DFSTTLNALA DQISLEKMIK ISYNFLHSIN GQKGKL 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW35226.1.
RefSeqYP_178891.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HUZ4.
SMRQ5HUZ4. Positions 1-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE0889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW35226; AAW35226; CJE0889.
GeneID3231402.
KEGGcjr:CJE0889.
PATRIC20043545. VBICamJej134361_0902.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000102494.
KOK01921.
OMAMEFCVLF.
OrthoDBEOG6ND0KB.
ProtClustDBPRK01966.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-909-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_CAMJR
AccessionPrimary (citable) accession number: Q5HUZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 71 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