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Protein

D-alanine--D-alanyl carrier protein ligase

Gene

dltA

Organism
Listeria monocytogenes serotype 4b (strain F2365)
Status
Reviewed-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 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 sitei202D-alanineUniRule annotation1
Binding sitei306D-alanine; via carbonyl oxygenUniRule annotation1
Binding sitei389ATPUniRule annotation1
Binding sitei498ATPUniRule annotation1
Binding sitei498D-alanineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi157 – 158ATPUniRule annotation2
Nucleotide bindingi297 – 302ATPUniRule annotation6

GO - Molecular functioni

  • acid-amino acid ligase activity Source: JCVI
  • AMP binding Source: JCVI
  • ATP binding Source: UniProtKB-KW
  • D-alanine [D-alanyl carrier protein] ligase activity Source: InterPro
  • transmembrane transporter activity Source: JCVI

GO - Biological processi

  • lipoteichoic acid biosynthetic process Source: UniProtKB-UniPathway
  • peptidoglycan biosynthetic process Source: JCVI

Keywordsi

Molecular functionLigase
LigandATP-binding, 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 annotation
Ordered Locus Names:LMOf2365_0994
OrganismiListeria monocytogenes serotype 4b (strain F2365)
Taxonomic identifieri265669 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002131471 – 510D-alanine--D-alanyl carrier protein ligaseAdd BLAST510

Proteomic databases

PRIDEiQ721J2

Structurei

3D structure databases

ProteinModelPortaliQ721J2
SMRiQ721J2
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
IPR020845 AMP-binding_CS
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
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit

Sequencei

Sequence statusi: Complete.

Q721J2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSIIERID AWAEKTPDFP CYEYAGTRLS YKELKRQSDA FGSFLLKNLN
60 70 80 90 100
TDKEKPIIVY GHMSPLMLVA FLGSIKSGRA YVPVDVSMPV ERIEQIKKAA
110 120 130 140 150
DPSLFICTEE LPSNLTITGC PVLTQDQLMD ALEKHFGEVP DKEACVKNDD
160 170 180 190 200
NYYIIYTSGS TGNPKGVQIS QNNLVSFSNW ILQDFSLSQG LRFLNQAPFS
210 220 230 240 250
FDLSVMDLYP SLLSGGTLVP LDKTITANMK DLYREIPAQN LDVWVSTPSF
260 270 280 290 300
ADLCLLDDNF NQENNPGLIR FLFCGEVLAK KTASELLNRF PDAVIYNTYG
310 320 330 340 350
PTEATVAVTQ VKVTREVIDA YPSLPLGVIK PDMRLHIVDQ ETGEVLPEGE
360 370 380 390 400
KGEIVLIGAS VSKGYLNEPE KTDQVFFDYK GYQAYRTGDS GIIKDGYLFF
410 420 430 440 450
QGRLDFQIKL HGYRIELEDI ENNLKKVSYI QNCAIIPKMK DEKVDMLVAQ
460 470 480 490 500
VIPTNHDFEK EYQLSAAIKN ELKEFMPAYM IPRKWIYKTE FPLTMNGKID
510
RKALNSEVNK
Length:510
Mass (Da):57,613
Last modified:July 5, 2004 - v1
Checksum:i8AE9326D9D3A8FE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017262 Genomic DNA Translation: AAT03772.1
RefSeqiWP_003727064.1, NC_002973.6

Genome annotation databases

EnsemblBacteriaiAAT03772; AAT03772; LMOf2365_0994
KEGGilmf:LMOf2365_0994

Similar proteinsi

Entry informationi

Entry nameiDLTA_LISMF
AccessioniPrimary (citable) accession number: Q721J2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: May 23, 2018
This is version 84 of the entry and version 1 of the sequence. See 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

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