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Q65N65 (DDL_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. 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:BLi00543, BL02193
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length361 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 – 361361D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000030426

Regions

Domain140 – 345206ATP-grasp
Nucleotide binding173 – 22856ATP By similarity

Sites

Metal binding2991Magnesium or manganese 1 By similarity
Metal binding3121Magnesium or manganese 1 By similarity
Metal binding3121Magnesium or manganese 2 By similarity
Metal binding3141Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65N65 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: DA83B729D1862A9B

FASTA36140,057
        10         20         30         40         50         60 
MKTRLGLVYG GKSAEHNVSL QTALAVTKAL DTEKFDIHPI YITEKGEWVR GPQLTEPVSN 

        70         80         90        100        110        120 
VKMLQFEQTG QTFSPAVLNR DMFPGEADAK EDSIDVVFPL LHGPNGEDGT IQGMLELLNV 

       130        140        150        160        170        180 
PYVGNGVLAS SAGMDKVVMK HLFAQAGLDQ AKYVSFLKKT WSQSKEECYA QVEGELGYPC 

       190        200        210        220        230        240 
FVKPANLGSS VGISKCRSRE ELDQAFELAF QYDRKIVVEE GVIGREIELG VLGNDEPVCS 

       250        260        270        280        290        300 
VAGEIAPKKD FYDYKAKYED GDTDLIIPAS LTEDEYETMR SMAVKAFQAI DGSGLVRADF 

       310        320        330        340        350        360 
FLTNEGRVLI NEVNTMPGFT PFSMFPLLWK QSGVEYAELI EKLVALAIER HEEKQQIKHT 


F 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU22144.1.
AE017333 Genomic DNA. Translation: AAU39499.1.
RefSeqYP_006711970.1. NC_006322.1.
YP_077782.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65N65.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL02193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU22144; AAU22144; BL02193.
AAU39499; AAU39499; BLi00543.
GeneID3030394.
3099263.
KEGGbld:BLi00543.
bli:BL02193.
PATRIC18946603. VBIBacLic203714_0540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011593.
KOK01921.
OMAQIDVIFP.
OrthoDBEOG64BQ73.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-535-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
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_BACLD
AccessionPrimary (citable) accession number: Q65N65
Secondary accession number(s): Q62YL4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 79 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