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O51927 (DDL_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:ddlB
Ordered Locus Names:BUsg_208
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length306 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 – 306306D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_0000177798

Regions

Domain101 – 303203ATP-grasp
Nucleotide binding134 – 18956ATP By similarity

Sites

Active site151 By similarity
Active site1501 By similarity
Active site2811 By similarity
Metal binding2571Magnesium or manganese 1 By similarity
Metal binding2701Magnesium or manganese 1 By similarity
Metal binding2701Magnesium or manganese 2 By similarity
Metal binding2721Magnesium or manganese 2 By similarity

Experimental info

Sequence conflict12 – 132NS → IL in AAC46067. Ref.1
Sequence conflict287 – 2915AKSIG → SKKYR in AAC46067. Ref.1
Sequence conflict295 – 2962DE → VN in AAC46067. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O51927 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 0AA64721CCEBD515

FASTA30634,388
        10         20         30         40         50         60 
MKKKIAVLLG GNSSERKISI KSGYAILQSL LRSGFNAYAI DTRDFPIMQL KKQGFDSAYI 

        70         80         90        100        110        120 
ALHGTGGEDG SIQGILEYLN IPYTGSGIMS SAISLDKWRT KLLWKSLSLR VLPDIYLQKK 

       130        140        150        160        170        180 
DISKYTYSYI LKKILKLKFP VVIKPNNAGS SIGITIVNHP DLLIDSINLA FNYSNNIIIE 

       190        200        210        220        230        240 
KFLKGTEYTV SILNKKVLPP IKIITKNNFY DYSSKYIESS TEYICPSGLN YQKEEELKKI 

       250        260        270        280        290        300 
VEIAWNSLGC KGCGRIDAIL DNKDKFWLLE INTIPGMTHR SLVPMAAKSI GISFDELILK 


ILKINK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of ftsZ, the cell division gene of Buchnera aphidicola (endosymbiont of aphids) and detection of the product."
Baumann L., Baumann P.
Curr. Microbiol. 36:85-89(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF012886 Genomic DNA. Translation: AAC46067.1.
AE013218 Genomic DNA. Translation: AAM67772.1.
RefSeqNP_660561.1. NC_004061.1.

3D structure databases

ProteinModelPortalO51927.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67772; AAM67772; BUsg_208.
GeneID1005405.
KEGGbas:BUsg208.
PATRIC21247203. VBIBucAph100086_0215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
KOK01921.
OMADTQYRIP.
OrthoDBEOG6ND0KB.
ProtClustDBPRK01372.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-218-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_BUCAP
AccessionPrimary (citable) accession number: O51927
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 30, 2002
Last modified: February 19, 2014
This is version 101 of the entry and version 2 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names