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Q1LT82 (DDL_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:BCI_0388
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length375 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 – 375375D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000030431

Regions

Domain145 – 348204ATP-grasp
Nucleotide binding175 – 23056ATP By similarity

Sites

Metal binding3021Magnesium or manganese 1 By similarity
Metal binding3151Magnesium or manganese 1 By similarity
Metal binding3151Magnesium or manganese 2 By similarity
Metal binding3171Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LT82 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 11B78F1FC8877C53

FASTA37541,589
        10         20         30         40         50         60 
MAKLRVGIIF GGQSAEHEVS LQSAKNIVET IDENKFEVVL FGIDKEGQWH INNKLNYLIY 

        70         80         90        100        110        120 
GENETYIALN KSNKHIAIIP GRKHDQFIQI DMLEQLVQLD VIFPIVHGTL GEDGNLQGLL 

       130        140        150        160        170        180 
RMANLPFVGS TVLGSAVSMD KDIAKRLLRD ADLEVTPSIT LTRINRENFS YDQIITYLGS 

       190        200        210        220        230        240 
SLFVKPANQG SSVGVSKVIN RISFDQALAL AFCFDDKVLV ESAINGRELE CAVLGNHDPQ 

       250        260        270        280        290        300 
ASLCGEIVLS DNFYSYEKKY LNEHGAVVVV PAAISKEVSN NIQKIAVRAF QALNCTGMAR 

       310        320        330        340        350        360 
VDVFLTTNNK VLVNEVNTSP GFTSISMYPK LWQASGISYP ALITRLIELA IERYYAEQKK 

       370 
ISHRDIYNKI DTGSA 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF14027.1.
RefSeqYP_588832.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LT82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374463.BCI_0388.

Proteomic databases

PRIDEQ1LT82.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF14027; ABF14027; BCI_0388.
GeneID4056458.
KEGGbci:BCI_0388.
PATRIC21074283. VBIBauCic75062_0371.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011593.
KOK01921.
OMAQIDVIFP.
OrthoDBEOG64BQ73.

Enzyme and pathway databases

BioCycBCIC374463:GI6Q-388-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_BAUCH
AccessionPrimary (citable) accession number: Q1LT82
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: May 14, 2014
This is version 59 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