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A1UEB6 (DDL_MYCSK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:Mkms_1975
OrganismMycobacterium sp. (strain KMS) [Complete proteome] [HAMAP]
Taxonomic identifier189918 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length371 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 – 371371D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000057326

Regions

Domain154 – 361208ATP-grasp
Nucleotide binding182 – 23756ATP By similarity

Sites

Metal binding3161Magnesium or manganese 1 By similarity
Metal binding3281Magnesium or manganese 1 By similarity
Metal binding3281Magnesium or manganese 2 By similarity
Metal binding3301Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1UEB6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 076FA163DF19302A

FASTA37139,213
        10         20         30         40         50         60 
MIARNQRTRV AVVYGGRSSE HAISCVSAGS ILRNLDPERF DVVAVGITPD GSWVLTDGRP 

        70         80         90        100        110        120 
ETLAITDGRL PEVSAESGTA LALPADPGRR GELVSLSPAA AGEVLAAVDV VFPVLHGPYG 

       130        140        150        160        170        180 
EDGTIQGLLE LAGVPYVGAG VLASAAGMDK EFTKKLLVAE GLPVGDHVVL RPGRANVTLD 

       190        200        210        220        230        240 
ERERLGLPVF VKPARGGSSI GVSRVSDWAE LPAAIEAARR HDPKVIVEAG IAGRELECGV 

       250        260        270        280        290        300 
LEYPDGRVDA STIGEIRVAG VRGREDGFYD FATKYLDDGA ELDVPAKVED DVADEIRRLA 

       310        320        330        340        350        360 
IRAFRAIDCQ GLARVDFFLT DDGPVVNEIN TMPGFTTISM YPRMWAASGV DYPTLLAAMV 

       370 
DTAVARGTGL R 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. KMS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KMS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000518 Genomic DNA. Translation: ABL91174.1.
RefSeqYP_937964.1. NC_008705.1.

3D structure databases

ProteinModelPortalA1UEB6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189918.Mkms_1975.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL91174; ABL91174; Mkms_1975.
GeneID4613723.
KEGGmkm:Mkms_1975.
PATRIC18102866. VBIMycSp70743_2475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011593.
KOK01921.
OMAMDKIAMK.
OrthoDBEOG64BQ73.
ProtClustDBPRK01966.

Enzyme and pathway databases

BioCycMSP189918:GH4X-1988-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_MYCSK
AccessionPrimary (citable) accession number: A1UEB6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 56 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