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A5HYZ6 (DDL_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:CBO0452, CLC_0526
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Reference proteome] [HAMAP]
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length300 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 – 300300D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000030439

Regions

Domain99 – 293195ATP-grasp
Nucleotide binding126 – 18156ATP By similarity

Sites

Metal binding2481Magnesium or manganese 1 By similarity
Metal binding2601Magnesium or manganese 1 By similarity
Metal binding2601Magnesium or manganese 2 By similarity
Metal binding2621Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5HYZ6 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 7574E8A8FAA8E0E2

FASTA30033,349
        10         20         30         40         50         60 
MKIGVIMGGI STEREVSLNS GREVIKYLEL LEHEIIPIII DKKEDVMEKA KGIDFAFLAL 

        70         80         90        100        110        120 
HGKFGEDGTV QSVLQTLDIP YSGCGPLTSA ICMDKDMTKK ILKYANINTA DWVNVSSVEN 

       130        140        150        160        170        180 
IDYEAIEKIG YPVFVKPNSG GSSVATNLVK DKEGIKEAVE LALKYDKEVM IENYTKGEEI 

       190        200        210        220        230        240 
TCCMLNGKML PVLAIRPHAE FFDYTAKYAD GGSDEVVIEL EENLHKKVEE MALACWKELK 

       250        260        270        280        290        300 
CEVYVRVDMI VKDGIPYVLE LNTLPGMTKN SLFPKSANAV GISFAELLNS IVKYSLEVER 

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000727 Genomic DNA. Translation: ABS38753.1.
AM412317 Genomic DNA. Translation: CAL82005.1.
RefSeqYP_001252996.1. NC_009495.1.
YP_001386411.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5HYZ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413999.CBO0452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS38753; ABS38753; CLC_0526.
GeneID5184707.
5401669.
KEGGcbh:CLC_0526.
cbo:CBO0452.
PATRIC19363021. VBICloBot22612_0455.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCBOT413999:GJ72-513-MONOMER.
CBOT441771:GIWX-497-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_CLOBH
AccessionPrimary (citable) accession number: A5HYZ6
Secondary accession number(s): A7G0Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: February 19, 2014
This is version 53 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