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Q5XBN5 (DLTA_STRP6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:M6_Spy1043
OrganismStreptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394) [Complete proteome] [HAMAP]
Taxonomic identifier286636 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length512 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.

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
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512D-alanine--poly(phosphoribitol) ligase subunit 1 HAMAP-Rule MF_00593
PRO_0000213167

Secondary structure

1 ............................................................................................... 512
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5XBN5 [UniParc].

Last modified November 23, 2004. 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]"Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain."
Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.
J. Infect. Dis. 190:727-738(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-946 / MGAS10394.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000003 Genomic DNA. Translation: AAT87178.1.
RefSeqYP_060361.1. NC_006086.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L8CX-ray2.41A/B3-512[»]
ProteinModelPortalQ5XBN5.
ModBaseSearch...

Protein-protein interaction databases

STRING286636.M6_Spy1043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT87178; AAT87178; M6_Spy1043.
GeneID2941773.
KEGGspa:M6_Spy1043.
PATRIC19724266. VBIStrPyo30273_1078.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1020.
HOGENOMHOG000229995.
KOK03367.
OMAFCQEKMP.
ProtClustDBPRK04813.

Enzyme and pathway databases

UniPathwayUPA00556.

Family and domain databases

HAMAPMF_00593. DltA.
InterProIPR010071. AA_adenyl_domain.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. D_ala_DACP_lig.
[Graphical view]
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...

Other

EvolutionaryTraceQ5XBN5.

Entry information

Entry nameDLTA_STRP6
AccessionPrimary (citable) accession number: Q5XBN5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 23, 2004
Last modified: May 1, 2013
This is version 62 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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