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Q81IU1 (DDLB_BACCR) 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 B

EC=6.3.2.4
Alternative name(s):
D-Ala-D-Ala ligase B
D-alanylalanine synthetaseB
Gene names
Name:ddlB
Ordered Locus Names:BC_0257
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length361 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 – 361361D-alanine--D-alanine ligase B HAMAP-Rule MF_00047
PRO_0000177783

Regions

Domain140 – 345206ATP-grasp
Nucleotide binding173 – 22856ATP By similarity

Sites

Metal binding2991Magnesium or manganese 1 By similarity
Metal binding3121Magnesium or manganese 1 By similarity
Metal binding3121Magnesium or manganese 2 By similarity
Metal binding3141Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81IU1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 885D9E7C8FDC9214

FASTA36140,073
        10         20         30         40         50         60 
MTKIKLGLLY GGKSAEHQVS LQTALAAIKA LNQDKFEIHP IYITEQGQWV RGERIEGEVT 

        70         80         90        100        110        120 
DVEALKMSGA ENAISPLSLS TEIIPSAASE ENAIDVIFPL LHGPNGEDGT VQGLLELMNI 

       130        140        150        160        170        180 
PYVGNGVLAS SAGMDKVVMK NIFAEAGLKQ AKYASFIRSA WEKNREEAYS KVEDKLGYPC 

       190        200        210        220        230        240 
FVKPANLGSS VGINKCKNRE ELEDAFVEAF QFDRKIIVEE NIVGREVEVG VLGNDEPKCS 

       250        260        270        280        290        300 
VVGEIVPKKD FYDYKSKYID GDTALIIPAE MTEEESNVIK RDAIIAFQSL DGAGLTRADF 

       310        320        330        340        350        360 
FLTKDGEVYI NEVNTMPGFT PFSMFPLLWQ HTGLPYPELI EELIRLAIER HEEKQKIKYT 


I 

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References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP07326.1.
RefSeqNP_830125.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ81IU1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC0257.

Proteomic databases

PRIDEQ81IU1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP07326; AAP07326; BC_0257.
GeneID1202610.
KEGGbce:BC0257.
PATRIC32596142. VBIBacCer54481_0257.

Phylogenomic databases

eggNOGCOG1181.
KOK01921.
OMAKLAFQYD.
OrthoDBEOG64BQ73.

Enzyme and pathway databases

BioCycBCER226900:GJEU-259-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 nameDDLB_BACCR
AccessionPrimary (citable) accession number: Q81IU1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
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