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Q2FZW6 (DLTA_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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--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:SAOUHSC_00869
OrganismStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length485 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
Reference 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_0000289546

Sequences

Sequence LengthMass (Da)Tools
Q2FZW6 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: FFA535607F1FD328

FASTA48554,670
        10         20         30         40         50         60 
MTDIINKLQA FADANPQSIA VRHTTDELTY QQLMDESSKL AHRLQGSKKP MILFGHMSPY 

        70         80         90        100        110        120 
MIVGMIGAIK AGCGYVPVDT SIPEDRIKMI INKVQPEFVF NTTDESFESL EGEVFTIEDI 

       130        140        150        160        170        180 
KTSQDPVIFD SQIKDNDTVY TIFTSGSTGE PKGVQIEYAS LVQFTEWMLE LNKSGNEQQW 

       190        200        210        220        230        240 
LNQAPFSFDL SVMAIYPCLA SGGTLNLVDK NMINKPKLLN EMLTATPINI WVSTPSFMEM 

       250        260        270        280        290        300 
CLLLPTLNEE QYGSLNEFFF CGEILPHRAA KALVNRFPSA TIYNTYGPTE ATVAVTSIQI 

       310        320        330        340        350        360 
TQEILDQYPT LPVGVERPGA RLSTTDEGEL VIEGQSVSLG YLKNDQKTAE VFNFDDGIRT 

       370        380        390        400        410        420 
YHTGDKAKFE NGQWFIQGRI DFQIKLNGYR MELEEIETQL RQSEFVKEAI VVPVYKNDKV 

       430        440        450        460        470        480 
IHLIGAIVPT TEVTDNAEMT KNIKNDLKSR LPEYMIPRKF EWMEQLPLTS NGKIDRKKIA 


EVING 

« Hide

References

« Hide 'large scale' references
[1]"Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides."
Peschel A., Otto M., Jack R.W., Kalbacher H., Jung G., Goetz F.
J. Biol. Chem. 274:8405-8410(1999) [PubMed: 10085071] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF101234 Genomic DNA. Translation: AAD21957.1.
CP000253 Genomic DNA. Translation: ABD29994.1.
RefSeqYP_499422.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2FZW6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2FZW6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000029972; EBSTAP00000028923; EBSTAG00000029970.
GeneID3919216.
GenomeReviewsGene locus SAOUHSC_00869 in contig CP000253_GR.
KEGGsao:SAOUHSC_00869.
PATRIC19579256. VBIStaAur99865_0789.

Phylogenomic databases

eggNOGCOG1020.
GeneTreeEBGT00050000024490.
HOGENOMHBG320748.
OMAWIYKTEF.
ProtClustDBPRK04813.

Enzyme and pathway databases

BioCycSAUR93061:SAOUHSC_00869-MONOMER.

Family and domain databases

HAMAPMF_00593. DltA.
[Tree]
InterProIPR010071. AA_adenyl_domain.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLTA_STAA8
AccessionPrimary (citable) accession number: Q2FZW6
Secondary accession number(s): P68877, Q53661, Q9S673
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 21, 2006
Last modified: January 25, 2012
This is version 41 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