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C3PMU6 (DDL_RICAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:RAF_ORF0310
OrganismRickettsia africae (strain ESF-5) [Complete proteome] [HAMAP]
Taxonomic identifier347255 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length321 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 – 321321D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000202204

Regions

Domain121 – 315195ATP-grasp
Nucleotide binding147 – 19953ATP By similarity

Sites

Metal binding2681Magnesium or manganese 1 By similarity
Metal binding2821Magnesium or manganese 1 By similarity
Metal binding2821Magnesium or manganese 2 By similarity
Metal binding2841Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
C3PMU6 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 90C75F677CD30BBC

FASTA32136,022
        10         20         30         40         50         60 
MHKYQTHWVE HSIVKILSST GKKHIALMVG GMSAEREVSL VSSEGVSKAL IELGYRVTFI 

        70         80         90        100        110        120 
DMGADIAVRL QEIKPDIVFN CLHGTYGEDG CLPGLLNIMR IPYTHSGMLS SALAFDKIHS 

       130        140        150        160        170        180 
RIWFLTNNIN MAESIVVNKS DNIKNDPMKR PYVIKPLTQG SSIGVEVIFA EDDFNFADYD 

       190        200        210        220        230        240 
FPYGDQVIIE QYIKGRELQV AVLNGKALGA LEIKLLKNRF YDYETKYTEG FADHLCPAPL 

       250        260        270        280        290        300 
PANLYEKLLI ESEKIYKTMN CKGPARAEFI LEEQTNKLYA LEINTHPGMT PLSIVPEIAA 

       310        320 
YAGINFTNLI EEIIKMASFE S 

« Hide

References

[1]"Analysis of the Rickettsia africae genome reveals that virulence acquisition in Rickettsia species may be explained by genome reduction."
Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.
BMC Genomics 10:166-166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ESF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001612 Genomic DNA. Translation: ACP53256.1.
RefSeqYP_002844999.1. NC_012633.1.

3D structure databases

ProteinModelPortalC3PMU6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347255.RAF_ORF0310.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP53256; ACP53256; RAF_ORF0310.
GeneID7815310.
KEGGraf:RAF_ORF0310.
PATRIC17872465. VBIRicAfr6986_0372.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011592.
KOK01921.
OMAKYTEGFA.
OrthoDBEOG6ND0KB.
ProtClustDBPRK01372.

Enzyme and pathway databases

BioCycRAFR347255:GJCT-294-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. 2 hits.
[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_RICAE
AccessionPrimary (citable) accession number: C3PMU6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: February 19, 2014
This is version 40 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