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Q2S0H9 (Q2S0H9_SALRD) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
D-alanine--D-alanine ligase HAMAP-Rule MF_00047

EC=6.3.2.4 HAMAP-Rule MF_00047
Alternative name(s):
D-Ala-D-Ala ligase HAMAP-Rule MF_00047
D-alanylalanine synthetase HAMAP-Rule MF_00047
Gene names
Name:ddl HAMAP-Rule MF_00047
Ordered Locus Names:SRU_2197 EMBL ABC45025.1
OrganismSalinibacter ruber (strain DSM 13855 / M31) [Reference proteome] [HAMAP] EMBL ABC45025.1
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cell wall formation By similarity. HAMAP-Rule MF_00047 SAAS SAAS011095

Catalytic activity

ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. HAMAP-Rule MF_00047 SAAS SAAS011095

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity. HAMAP-Rule MF_00047 SAAS SAAS011095

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00047 SAAS SAAS011095

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00047 SAAS SAAS011095.

Sequence similarities

Belongs to the D-alanine--D-alanine ligase family. HAMAP-Rule MF_00047

Contains 1 ATP-grasp domain. HAMAP-Rule MF_00047

Contains ATP-grasp domain. SAAS SAAS011095

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain171 – 399229ATP-grasp By similarity HAMAP-Rule MF_00047
Nucleotide binding204 – 25956ATP By similarity HAMAP-Rule MF_00047

Sites

Metal binding3561Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047
Metal binding3701Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047
Metal binding3701Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047
Metal binding3721Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047

Sequences

Sequence LengthMass (Da)Tools
Q2S0H9 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 2FC52A6406D6EB46

FASTA43447,045
        10         20         30         40         50         60 
MPPSASFCFS SVPGPTVSSE PLQVGIVLGG VAPEHEVSVI TALQAAAALD RDRYTPVPIY 

        70         80         90        100        110        120 
VAKDGTWYTG DALLEVEAYR DLDALREDAL PVALAPTPYG HLELLEDRAP GILKRLQRPA 

       130        140        150        160        170        180 
LRRRIDVMLL GLHGGPGENG GVQGLCETFN VPYTSAGVFG SALGMDKVMS KRVCRQAGIP 

       190        200        210        220        230        240 
VVDFVALREG EWAGREAAAL DECEATLDYP LVVKPARCGS SIGIAQVNTR AELDAAIEDA 

       250        260        270        280        290        300 
LRYDDKVVVE KAVEALREIN CSVLGDGHEA TPSVLEEPVP SDDDAVLTFQ DKYMREDGEA 

       310        320        330        340        350        360 
AKAEGGTKSA ESSPEGMAAQ DRIVPANLSD ERTETIQDLA VRIFHQFECA GVVRIDFMID 

       370        380        390        400        410        420 
ESTGRVYFNE INTIPGSFSF YLWEPSGVSF DALVDRLVTI ARRRHRDRNG RVQTYDVNLL 

       430 
AEKNLQGVKA DEAP 

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References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC45025.1.
RefSeqYP_446302.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S0H9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309807.SRU_2197.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC45025; ABC45025; SRU_2197.
GeneID3852328.
KEGGsru:SRU_2197.
PATRIC23426927. VBISalRub86502_2286.

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011593.
KOK01921.
OMAMANQKLT.
OrthoDBEOG64BQ73.
PhylomeDBQ2S0H9.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-2195-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. 2 hits.
PF01820. Dala_Dala_lig_N. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 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 nameQ2S0H9_SALRD
AccessionPrimary (citable) accession number: Q2S0H9
Entry history
Integrated into UniProtKB/TrEMBL: January 24, 2006
Last sequence update: January 24, 2006
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)