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Protein

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

Gene

dltA

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed-Annotation score: Annotation score: 3 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 - Biological processi

Virulence

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciLMON169963:LMO0974-MONOMER.
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
Ordered Locus Names:lmo0974
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
Proteomesi
  • UP000000817 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510D-alanine--poly(phosphoribitol) ligase subunit 1PRO_0000213148Add
BLAST

Proteomic databases

PaxDbiQ8Y8D4.

Interactioni

Protein-protein interaction databases

STRINGi169963.lmo0974.

Structurei

3D structure databases

ProteinModelPortaliQ8Y8D4.
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.
HOGENOMiHOG000229995.
KOiK03367.
OMAiLFICTEE.
PhylomeDBiQ8Y8D4.

Family and domain databases

HAMAPiMF_00593. DltA. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
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.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8Y8D4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSIIERID AWAEKTPDFP CYEYAGTRLS YKELKRQSDA FGSFLLKNLI
60 70 80 90 100
TDKEKPIIVY GHMSPLMLVA FLGSIKSGRA YVPVDVSMPV ERIEQIKKAA
110 120 130 140 150
DPSMFICTEE LPNNLTITGC PVLTQDQLMD ALEKHFGEVP DKEACVNNDD
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
ADLCLLDENF NQENNPRLTR FLFCGEVLAK KTASELLDRF PDAVIYNTYG
310 320 330 340 350
PTEATVAVTQ VKVTREIIDA 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
VIPTTHDFEK EYQLSAAIKK ELKEFMPAYM IPRKWIYKTD FPLTMNGKID
510
RKSLNSEVNK
Length:510
Mass (Da):57,762
Last modified:March 1, 2002 - v1
Checksum:i06A07EC2D32EF3D7
GO

Sequence cautioni

The sequence CAB51919 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti499 – 4991I → V in CAB51919 (PubMed:11849532).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012255 Genomic DNA. Translation: CAB51919.1. Different initiation.
AL591977 Genomic DNA. Translation: CAC99052.1.
PIRiAF1196.
RefSeqiNP_464499.1. NC_003210.1.
WP_003732429.1. NC_003210.1.

Genome annotation databases

EnsemblBacteriaiCAC99052; CAC99052; CAC99052.
GeneIDi986449.
KEGGilmo:lmo0974.
PATRICi20311046. VBILisMon69206_1001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012255 Genomic DNA. Translation: CAB51919.1. Different initiation.
AL591977 Genomic DNA. Translation: CAC99052.1.
PIRiAF1196.
RefSeqiNP_464499.1. NC_003210.1.
WP_003732429.1. NC_003210.1.

3D structure databases

ProteinModelPortaliQ8Y8D4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi169963.lmo0974.

Proteomic databases

PaxDbiQ8Y8D4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC99052; CAC99052; CAC99052.
GeneIDi986449.
KEGGilmo:lmo0974.
PATRICi20311046. VBILisMon69206_1001.

Phylogenomic databases

eggNOGiENOG4108IQD. Bacteria.
COG1020. LUCA.
HOGENOMiHOG000229995.
KOiK03367.
OMAiLFICTEE.
PhylomeDBiQ8Y8D4.

Enzyme and pathway databases

UniPathwayiUPA00556.
BioCyciLMON169963:LMO0974-MONOMER.

Family and domain databases

HAMAPiMF_00593. DltA. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
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.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDLTA_LISMO
AccessioniPrimary (citable) accession number: Q8Y8D4
Secondary accession number(s): Q9S391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: March 1, 2002
Last modified: September 7, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.