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Protein

D-alanine--poly(phosphoribitol) ligase subunit 1

Gene

dltA

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

Pathwayi: lipoteichoic acid biosynthesis

This protein is involved in the pathway lipoteichoic acid biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway lipoteichoic acid biosynthesis and in Cell wall biogenesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00556.

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanine--poly(phosphoribitol) ligase subunit 1UniRule annotation (EC:6.1.1.13UniRule annotation)
Alternative name(s):
D-alanine-D-alanyl carrier protein ligaseUniRule annotation
Short name:
DCLUniRule annotation
D-alanine-activating enzymeUniRule annotation
Short name:
DAEUniRule annotation
Gene namesi
Name:dltAUniRule annotation
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002131521 – 485D-alanine--poly(phosphoribitol) ligase subunit 1Add BLAST485

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL0935.

Structurei

3D structure databases

ProteinModelPortaliP0C397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQD. Bacteria.
COG1020. LUCA.

Family and domain databases

HAMAPiMF_00593. DltA. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. DltA.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
TIGR01734. D-ala-DACP-lig. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDIINKLQA FADANPQSIA VRHTTDELTY QQLMDESSKL AHRLQGSKKP
60 70 80 90 100
MILFGHMSPY MIVGMIGAIK AGCGYVPVDT SIPEDRIKMI INKVQPEFVF
110 120 130 140 150
NTTDESFESL EGEVFTIEDI KTSQDPVIFD SQIKDNDTVY TIFTSGSTGE
160 170 180 190 200
PKGVQIEYAS LVQFTEWMLE LNKSGNKQQW LNQAPFSFDL SVMAIYPCLA
210 220 230 240 250
SGGTLNLVDK NMINKPKLLN EMLTATPINI WVSTPSFMEM CLLLPTLNEE
260 270 280 290 300
QYGSLNEFFF CGEILPHRAA KALVSRFPSA TIYNTYGPTE ATVAVTSIQI
310 320 330 340 350
TQEILDQYPT LPVGVERLGA RLSTTDDGEL VIEGQSVSLG YLKNDQKTAE
360 370 380 390 400
VFNFDDGIRT YHTGDKAKFE NGQWFIQGRI DFQIKLNGYR MELEEIETQL
410 420 430 440 450
RQSEFVKEAI VVPVYKNDKV IHLIGAIVPT TEVTDNAEMT KNIKNDLKSR
460 470 480
LPEYMIPRKF EWMEQLPLTS NGKIDRKKIA EVING
Length:485
Mass (Da):54,644
Last modified:May 29, 2007 - v1
Checksum:i3E2DB528D8211794
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86240 Genomic DNA. Translation: BAA13059.2.
RefSeqiWP_000129659.1. NZ_MAQQ01000003.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86240 Genomic DNA. Translation: BAA13059.2.
RefSeqiWP_000129659.1. NZ_MAQQ01000003.1.

3D structure databases

ProteinModelPortaliP0C397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL0935.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108IQD. Bacteria.
COG1020. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00556.

Family and domain databases

HAMAPiMF_00593. DltA. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. DltA.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
TIGR01734. D-ala-DACP-lig. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDLTA_STAAU
AccessioniPrimary (citable) accession number: P0C397
Secondary accession number(s): P68877, Q53661, Q9S673
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: November 30, 2016
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.