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Protein

D-alanine--D-alanyl carrier protein ligase

Gene

dltA

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.UniRule annotation

Catalytic activityi

D-alanine + ATP + holo-[D-alanyl-carrier protein] = AMP + diphosphate + D-alanyl-[D-alanyl-carrier protein].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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei189D-alanineUniRule annotation1
Binding sitei293D-alanine; via carbonyl oxygenUniRule annotation1
Binding sitei365ATPUniRule annotation1
Binding sitei473ATPUniRule annotation1
Binding sitei473D-alanineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi144 – 145ATPUniRule annotation2
Nucleotide bindingi284 – 289ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayi
UPA00556

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanine--D-alanyl carrier protein ligaseUniRule annotation (EC:6.2.1.-UniRule annotation)
Short name:
DCLUniRule annotation
Alternative name(s):
D-alanine--poly(phosphoribitol) ligase subunit 1UniRule annotation
D-alanine-activating enzymeUniRule annotation
Short name:
DAEUniRule annotation
Gene namesi
Name:dltAUniRule annotation
Ordered Locus Names:SA0793
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002131511 – 485D-alanine--D-alanyl carrier protein ligaseAdd BLAST485

2D gel databases

SWISS-2DPAGEiP99107

Structurei

3D structure databases

ProteinModelPortaliP99107
SMRiP99107
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229995
KOiK03367
OMAiNFYIIFT

Family and domain databases

HAMAPiMF_00593 DltA, 1 hit
InterProiView protein in InterPro
IPR010071 AA_adenyl_domain
IPR025110 AMP-bd_C
IPR000873 AMP-dep_Synth/Lig
IPR010072 DltA
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
TIGRFAMsiTIGR01733 AA-adenyl-dom, 1 hit
TIGR01734 D-ala-DACP-lig, 1 hit

Sequencei

Sequence statusi: Complete.

P99107-1 [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:January 4, 2005 - v1
Checksum:i3E2DB528D8211794
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA Translation: BAB42032.1
PIRiE89859
RefSeqiWP_000129659.1, NC_002745.2

Genome annotation databases

EnsemblBacteriaiBAB42032; BAB42032; BAB42032
KEGGisau:SA0793

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA Translation: BAB42032.1
PIRiE89859
RefSeqiWP_000129659.1, NC_002745.2

3D structure databases

ProteinModelPortaliP99107
SMRiP99107
ModBaseiSearch...
MobiDBiSearch...

2D gel databases

SWISS-2DPAGEiP99107

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB42032; BAB42032; BAB42032
KEGGisau:SA0793

Phylogenomic databases

HOGENOMiHOG000229995
KOiK03367
OMAiNFYIIFT

Enzyme and pathway databases

UniPathwayi
UPA00556

Family and domain databases

HAMAPiMF_00593 DltA, 1 hit
InterProiView protein in InterPro
IPR010071 AA_adenyl_domain
IPR025110 AMP-bd_C
IPR000873 AMP-dep_Synth/Lig
IPR010072 DltA
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
TIGRFAMsiTIGR01733 AA-adenyl-dom, 1 hit
TIGR01734 D-ala-DACP-lig, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDLTA_STAAN
AccessioniPrimary (citable) accession number: P99107
Secondary accession number(s): Q53661
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: October 10, 2018
This is version 82 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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