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Reviewed, UniProtKB/Swiss-Prot Q4L4U5 (DLTA_STAHJ)

Last modified June 16, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    D-alanine--poly(phosphoribitol) ligase subunit 1
    EC=6.1.1.13
Alternative name(s):
    D-alanine-activating enzyme
      Short name=DAE
    D-alanine-D-alanyl carrier protein ligase
      Short name=DCL
Gene names
Name: dltA
Ordered Locus Names: SH2021
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 485485D-alanine--poly(phosphoribitol) ligase subunit 1 HAMAP MF_00593
PRO_0000213158

Sequences

Sequence LengthMass (Da)Tools
Q4L4U5-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 6724289A0688ABB3

FASTA48554,705
        10         20         30         40         50         60 
MTDIINLIND FGQSNPERVA VRHKDEELTY QQLMDESSKL AHLLQDNHKP LIVYGHMSPY 

        70         80         90        100        110        120 
MLVGMIGAIK AGCGYVPIDT SVPSERVNMI INKVQPDIIF NTSDTQLNHS NIQELTIQSI 

       130        140        150        160        170        180 
QDSDNPTLFD SQMGLTDVVY TIFTSGSTGE PKGVQIEYAS LIEFAEWMVS LNESEGSQEW 

       190        200        210        220        230        240 
LNQAPFSFDL SVMAIYPCLT SGGTLNLVDK EMINKPKLLN EMLVNTPINA WVSTPSFMEM 

       250        260        270        280        290        300 
CLLLPNLNES SYPSLNHFFF CGEILPHRTA KALLDRYPSA VVYNTYGPTE ATVAVTGIKL 

       310        320        330        340        350        360 
TPEVIEAYNP LPVGVSRPNT SLFTTDEGEL VIKGNSVSLG YLDNKEKTDA VFNFEDGLRI 

       370        380        390        400        410        420 
YHTGDKAIEK DGQWFIQGRI DFQIKLNGYR MELEEIETQL RQSEFVRETV VVPVYKNNKV 

       430        440        450        460        470        480 
IHLIGAVVPT EEVRDDLEMT RQIKSELKSR LPEYMIPRKF VWMKQLPLTS NGKLDRKQVA 


EDINA 

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References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP006716 Genomic DNA. Translation: BAE05330.1.
RefSeqYP_253936.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3482302.
GenomeReviewsGene locus SH2021 in contig AP006716_GR.
KEGGsha:SH2021.
NMPDRfig|279808.3.peg.2392.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ4L4U5.
OMAQ4L4U5. THIKHEL.

Enzyme and pathway databases

BioCycSHAE279808:SH2021-MON.

Family and domain databases

HAMAPMF_00593.
[Tree]
InterProIPR010071. AA_adenyl_domain.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. D_ala_DACP_lig.
[Graphical view]
PANTHERPTHR11968:SF34. D_ala_DACP_lig. 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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLTA_STAHJ
AccessionPrimary (citable) accession number: Q4L4U5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: August 2, 2005
Last modified: June 16, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents