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Q87HS0 (DDL_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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:VPA0886
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length329 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 – 329329D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_0000177902

Regions

Domain120 – 326207ATP-grasp
Nucleotide binding150 – 20556ATP By similarity

Sites

Metal binding2801Magnesium or manganese 1 By similarity
Metal binding2931Magnesium or manganese 1 By similarity
Metal binding2931Magnesium or manganese 2 By similarity
Metal binding2951Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87HS0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 00BD14677D80A2D5

FASTA32936,957
        10         20         30         40         50         60 
MIKNILLLCG GGSSEHEISL LSANFVEQQL NLIQNVKVTR VEIKNEGWVT DQGELVYLDL 

        70         80         90        100        110        120 
NTKQLCSNES NQTIDFIVPC IHGFPGETGD IQSLFEIAGI PYLGCGPEAS SNSFNKITSK 

       130        140        150        160        170        180 
LWYDALDIPN TPYLFLTRND EHAHRQAEQA FEKWGKVFVK AARQGSSVGC YSVAEKQAIA 

       190        200        210        220        230        240 
KAVNDAFGYS DQVLVEKAVK PRELEVAAYE MNGELHITKP GEVIAPDGAF YSYDEKYSSS 

       250        260        270        280        290        300 
SHSLTEVEAK NLTQEQIDKI RHASETVFKQ MNLRHLSRID FFLTEDNEIY LNEVNTFPGM 

       310        320 
TPISMFPKML QNNGHKFHEF LEDCINSAK 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000032 Genomic DNA. Translation: BAC62229.1.
RefSeqNP_800396.1. NC_004605.1.

3D structure databases

ProteinModelPortalQ87HS0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VPA0886.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC62229; BAC62229; BAC62229.
GeneID1191575.
KEGGvpa:VPA0886.
PATRIC20146173. VBIVibPar50997_3819.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011592.
KOK01921.
OMAMDKIAMK.
OrthoDBEOG6ND0KB.
ProtClustDBPRK01966.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-4119-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_VIBPA
AccessionPrimary (citable) accession number: Q87HS0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 76 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