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Protein

D-alanine--D-alanyl carrier protein ligase

Gene

dltA

Organism
Staphylococcus epidermidis
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

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 annotationSAAS annotation

Catalytic activityi

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

Pathwayi: lipoteichoic acid biosynthesis

This protein is involved in the pathway lipoteichoic acid biosynthesis, which is part of Cell wall biogenesis.UniRule annotationSAAS 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 functionLigaseUniRule annotationSAAS annotationImported
LigandATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00556.

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 annotationImported
ORF Names:CTJ04_10240Imported
OrganismiStaphylococcus epidermidisImported
Taxonomic identifieri1282 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

SMRiA0A2G7IVF1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 386AMP-bindingInterPro annotationAdd BLAST377
Domaini395 – 473AMP-binding_CInterPro annotationAdd BLAST79

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili386 – 406Sequence analysisAdd BLAST21

Sequence similaritiesi

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

Keywords - Domaini

Coiled coilSequence analysis

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.

A0A2G7IVF1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLINILNH FVQEQPEAVA VRHTNDELTY KQLDEESSKL AHLLQDSKKP
60 70 80 90 100
MILYGHMSPY MIVGMIGAIK SGCGYVPIDT SVPKERVNMI IDKVQPEIIF
110 120 130 140 150
NTSDETLEQT NAQVLKVSDI QDSQYPIVFD SQMKQNDVVY TIFTSGSTGE
160 170 180 190 200
PKGVQIEYAS LNEFAEWMVS LNKTGTGKEW LNQAPFSFDL SVMAIYPCLT
210 220 230 240 250
SGGTLNLVDK DMIKKPKLLN EMLVQTPMNV WVSTPSFIEM CLLLPNLNEQ
260 270 280 290 300
QYSSLKQFFF CGEILPHKTA KALVERFPNS MIYNTYGPTE ATVAVTSIQI
310 320 330 340 350
TEEILNQYNP LPVGVARPGT KLFATEEGEL VIEGQSVSLG YLKNEEKTTA
360 370 380 390 400
VFNFEDGVRT YHTGDKAKIE DGLWFIQGRI DFQIKLNGYR MELEEIETQL
410 420 430 440 450
RQSKHVREAV VVPVYKNGKV IHLIGAVVPT EPVEDNLAMT THIKHELKSR
460 470 480
LPEYMIPRKF EWMEQLPLTS NGKLDRKKIA EVVNG
Length:485
Mass (Da):54,796
Last modified:January 31, 2018 - v1
Checksum:iB4B4025BD61F5892
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
PEIW01000019 Genomic DNA. Translation: PIH21329.1.
RefSeqiWP_001831977.1. NZ_PIYR01000034.1.

Similar proteinsi

Entry informationi

Entry nameiA0A2G7IVF1_STAEP
AccessioniPrimary (citable) accession number: A0A2G7IVF1
Entry historyiIntegrated into UniProtKB/TrEMBL: January 31, 2018
Last sequence update: January 31, 2018
Last modified: March 28, 2018
This is version 3 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported