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Q81G39 (DLTA_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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--poly(phosphoribitol) ligase subunit 1

EC=6.1.1.13
Alternative name(s):
D-alanine-D-alanyl carrier protein ligase
Short name=DCL
D-alanine-activating enzyme
Short name=DAE
Gene names
Name:dltA
Ordered Locus Names:BC_1372
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Catalyzes an ATP-dependent two-step reaction where it forms a high energy D-alanyl AMP intermediate and transfers the alanyl residues from AMP to Dcp By similarity. HAMAP-Rule MF_00593

Catalytic activity

ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate). HAMAP-Rule MF_00593

Pathway

Cell wall biogenesis; lipoteichoic acid biosynthesis. HAMAP-Rule MF_00593

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00593.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. DltA subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipoteichoic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionAMP binding

Inferred from electronic annotation. Source: InterPro

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

D-alanine-poly(phosphoribitol) ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504D-alanine--poly(phosphoribitol) ligase subunit 1 HAMAP-Rule MF_00593
PRO_1000025526

Secondary structure

............................................................................................... 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q81G39 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 96BE762A25E315D2

FASTA50456,494
        10         20         30         40         50         60 
MKLLEQIEKW AAETPDQTAF VWRDAKITYK QLKEDSDALA HWISSEYPDD RSPIMVYGHM 

        70         80         90        100        110        120 
QPEMIINFLG CVKAGHAYIP VDLSIPADRV QRIAENSGAK LLLSATAVTV TDLPVRIVSE 

       130        140        150        160        170        180 
DNLKDIFFTH KGNTPNPEHA VKGDENFYII YTSGSTGNPK GVQITYNCLV SFTKWAVEDF 

       190        200        210        220        230        240 
NLQTGQVFLN QAPFSFDLSV MDIYPSLVTG GTLWAIDKDM IARPKDLFAS LEQSDIQVWT 

       250        260        270        280        290        300 
STPSFAEMCL MEASFSESML PNMKTFLFCG EVLPNEVARK LIERFPKATI MNTYGPTEAT 

       310        320        330        340        350        360 
VAVTGIHVTE EVLDQYKSLP VGYCKSDCRL LIMKEDGTIA PDGEKGEIVI VGPSVSVGYL 

       370        380        390        400        410        420 
GSPELTEKAF TMIDGERAYK TGDAGYVENG LLFYNGRLDF QIKLHGYRME LEEIEHHLRA 

       430        440        450        460        470        480 
CSYVEGAVIV PIKKGEKYDY LLAVVVPGEH SFEKEFKLTS AIKKELNERL PNYMIPRKFM 

       490        500 
YQSSIPMTPN GKVDRKKLLS EVTA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP08354.1.
RefSeqNP_831153.1. NC_004722.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DHVX-ray2.00A1-504[»]
3FCCX-ray2.32A1-504[»]
3FCEX-ray1.90A1-504[»]
ProteinModelPortalQ81G39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC1372.

Proteomic databases

PRIDEQ81G39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP08354; AAP08354; BC_1372.
GeneID1203721.
KEGGbce:BC1372.
PATRIC32598473. VBIBacCer54481_1346.

Phylogenomic databases

eggNOGCOG1020.
KOK03367.
OMAIANQAPF.
OrthoDBEOG6QP0WP.

Enzyme and pathway databases

BioCycBCER226900:GJEU-1372-MONOMER.
UniPathwayUPA00556.

Family and domain databases

HAMAPMF_00593. DltA.
InterProIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. D_ala_DACP_lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR01733. AA-adenyl-dom. 1 hit.
TIGR01734. D-ala-DACP-lig. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ81G39.

Entry information

Entry nameDLTA_BACCR
AccessionPrimary (citable) accession number: Q81G39
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 73 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways