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Q1JLB7 (DLTA_STRPC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:MGAS9429_Spy1115
OrganismStreptococcus pyogenes serotype M12 (strain MGAS9429) [Complete proteome] [HAMAP]
Taxonomic identifier370551 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 MF_00593

Catalytic activity

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

Pathway

Cell wall biogenesis; lipoteichoic acid biosynthesis. HAMAP MF_00593

Subcellular location

Cytoplasm Probable HAMAP 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 termComplete proteome
Gene Ontology (GO)
   Biological processteichoic acid biosynthetic process

Inferred from electronic annotation. Source: InterPro

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512D-alanine--poly(phosphoribitol) ligase subunit 1 HAMAP MF_00593
PRO_1000025537

Sequences

Sequence LengthMass (Da)Tools
Q1JLB7 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 330928DC894A6146

FASTA51256,987
        10         20         30         40         50         60 
MIKDMIDSIE QFAQTQADFP VYDCLGERRT YGQLKRDSDS IAAFIDSLAL LAKSPVLVFG 

        70         80         90        100        110        120 
AQTYDMLATF VALTKSGHAY IPVDVHSAPE RILAIIEIAK PSLIIAIEEF PLTIEGISLV 

       130        140        150        160        170        180 
SLSEIESAKL AEMPYERTHS VKGDDNYYII FTSGTTGQPK GVQISHDNLL SFTNWMIEDA 

       190        200        210        220        230        240 
AFDVPKQPQM LAQPPYSFDL SVMYWAPTLA LGGTLFALPK ELVADFKQLF TTIAQLPVGI 

       250        260        270        280        290        300 
WTSTPSFADM AMLSDDFCQA KMPALTHFYF DGEELTVSTA RKLFERFPSA KIINAYGPTE 

       310        320        330        340        350        360 
ATVALSAIEI TREMVDNYTR LPIGYPKPDS PTYIIDEDGK ELSSGEQGEI IVTGPAVSKG 

       370        380        390        400        410        420 
YLNNPEKTAE AFFTFKGQPA YHTGDIGSLT EDNILLYGGR LDFQIKYAGY RIELEDVSQQ 

       430        440        450        460        470        480 
LNQSPMVASA VAVPRYNKEH KVQNLLAYIV VKDGVKERFD RELELTKAIK ASVKDHMMSY 

       490        500        510 
MMPSKFLYRD SLPLTPNGKI DIKTLINEVN NR 

« Hide

References

[1]"Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus."
Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed: 16636287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS9429.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000259 Genomic DNA. Translation: ABF32302.1.
RefSeqYP_596846.1. NC_008021.1.

3D structure databases

ProteinModelPortalQ1JLB7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1JLB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000046114; EBSTRP00000044331; EBSTRG00000046106.
GeneID4060473.
GenomeReviewsGene locus MGAS9429_Spy1115 in contig CP000259_GR.
KEGGspk:MGAS9429_Spy1115.
PATRIC19753282. VBIStrPyo37061_1131.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1020.
GeneTreeEBGT00050000027070.
HOGENOMHBG320748.
OMAQISHANL.
ProtClustDBPRK04813.

Enzyme and pathway databases

BioCycSPYO370551:MGAS9429_SPY1115-MONOMER.

Family and domain databases

HAMAPMF_00593. DltA.
[Tree]
InterProIPR010071. AA_adenyl_domain.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. D_ala_DACP_lig.
[Graphical view]
KOK03367.
PANTHERPTHR24095:SF34. PTHR24095:SF34. 1 hit.
PfamPF00501. AMP-binding. 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...

Entry information

Entry nameDLTA_STRPC
AccessionPrimary (citable) accession number: Q1JLB7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 13, 2006
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families