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Q5PBK2 (DDL_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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:AM205
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length334 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 – 334334D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_0000341052

Regions

Domain110 – 306197ATP-grasp
Nucleotide binding138 – 19053ATP By similarity

Sites

Metal binding2581Magnesium or manganese 1 By similarity
Metal binding2721Magnesium or manganese 1 By similarity
Metal binding2721Magnesium or manganese 2 By similarity
Metal binding2741Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PBK2 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 223FB0FC1F3F40AF

FASTA33436,433
        10         20         30         40         50         60 
MPVSLARNAG MLSVAVLCGG SSPEREVSLA GGKRVADALG RLGYNATVLD LNRESVGQLL 

        70         80         90        100        110        120 
AMAPDLVYNA LHGVQGEDGC VSGLLDILGL ACTHSHVAAS SVGMDKVLTK HVLKSLGIDF 

       130        140        150        160        170        180 
PKFDVLTKEE LLSAKEVLPY PFVIKPVRGG STIGVHAIFS KSEYLDLSAH ADTLEDRMIV 

       190        200        210        220        230        240 
EEYVSGQEVQ TAVFLGRAIG TMELLFEGRI YSYDAKYVEG LCEHIFPANL PYDIYNLTLE 

       250        260        270        280        290        300 
WALKLHQCLG CKTLSRVDFR YDVANKALKL LEINTHPGMT VSSTLPEVLW LRCGLNFDHV 

       310        320        330 
VDLIVQDALG IDDSRRAYID ELMGKTVSRE PSHV 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86327.1.
RefSeqYP_153582.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5PBK2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234826.AM205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV86327; AAV86327; AM205.
GeneID3171882.
KEGGama:AM205.
PATRIC20946485. VBIAnaMar46146_0178.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011592.
KOK01921.
OMAANDTQYR.
OrthoDBEOG6ND0KB.

Enzyme and pathway databases

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.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS00843. DALA_DALA_LIGASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDDL_ANAMM
AccessionPrimary (citable) accession number: Q5PBK2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 83 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