UniProtKB - X5EMW7 (X5EMW7_STAAU)
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Protein
D-alanine--D-alanyl carrier protein ligase
Gene
dltA
Organism
Staphylococcus aureus
Status
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
: lipoteichoic acid biosynthesis Pathwayi
This protein is involved in the pathway lipoteichoic acid biosynthesis, which is part of Cell wall biogenesis.UniRule annotationSAAS annotationView all proteins of this organism that are known to be involved in the pathway lipoteichoic acid biosynthesis and in Cell wall biogenesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 189 | D-alanineUniRule annotation | 1 | |
Binding sitei | 293 | D-alanine; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 365 | ATPUniRule annotation | 1 | |
Binding sitei | 473 | ATPUniRule annotation | 1 | |
Binding sitei | 473 | D-alanineUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 144 – 145 | ATPUniRule annotation | 2 | |
Nucleotide bindingi | 284 – 289 | ATPUniRule annotation | 6 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- D-alanine [D-alanyl carrier protein] ligase activity Source: UniProtKB-UniRule
GO - Biological processi
- lipoteichoic acid biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | LigaseUniRule annotationSAAS annotationImported |
Ligand | ATP-bindingUniRule annotationSAAS annotation, 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 annotationImported ORF Names:B9Z08_03700Imported, EQ90_04305Imported, ERS072738_00109Imported, HMPREF3211_01980Imported |
Organismi | Staphylococcus aureusImported |
Taxonomic identifieri | 1280 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotationSAAS annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmUniRule annotationSAAS annotationFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 9 – 386 | AMP-bindingInterPro annotationAdd BLAST | 378 | |
Domaini | 395 – 473 | AMP-binding_CInterPro annotationAdd BLAST | 79 |
Sequence similaritiesi
Belongs to the ATP-dependent AMP-binding enzyme family. DltA subfamily.UniRule annotationSAAS annotation
Phylogenomic databases
KOi | K03367. |
Family and domain databases
HAMAPi | MF_00593. DltA. 1 hit. |
InterProi | View protein in InterPro IPR010071. AA_adenyl_domain. IPR025110. AMP-bd_C. IPR000873. AMP-dep_Synth/Lig. IPR010072. DltA. |
Pfami | View protein in Pfam PF00501. AMP-binding. 1 hit. PF13193. AMP-binding_C. 1 hit. |
TIGRFAMsi | TIGR01733. AA-adenyl-dom. 1 hit. TIGR01734. D-ala-DACP-lig. 1 hit. |
i Sequence
Sequence statusi: Complete.
X5EMW7-1 [UniParc]FASTAAdd to basket
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 LNKSGNEQQW LNQAPFSFDL SVMAIYPCLA
210 220 230 240 250
SGGTLNLVDK NMINKPKLLN EMLTATPINI WVSTPSFMEM CLLLPTLNEE
260 270 280 290 300
QYGSLNEFFF CGEILPHRAA KALVNRFPSA TIYNTYGPTE ATVAVTSIQI
310 320 330 340 350
TQEILDQYPT LPVGVERPGA RLSTTDEGEL 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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | FGBR01000001 Genomic DNA. Translation: CXL46552.1. LALJ01000006 Genomic DNA. Translation: KMR37401.1. LRQH01000146 Genomic DNA. Translation: KXA34243.1. NESW01000002 Genomic DNA. Translation: PHZ48736.1. |
RefSeqi | WP_000129653.1. NZ_PGGL01000001.1. |
Genome annotation databases
EnsemblBacteriai | CFF98890; CFF98890; ERS093009_00357. CXE18884; CXE18884; ERS074020_00104. CXL46552; CXL46552; ERS072738_00109. CZQ25806; CZQ25806; ERS1058648_00233. KXA34243; KXA34243; HMPREF3211_01980. OAP80407; OAP80407; A4U86_00805. SCR11086; SCR11086; SAMEA2298760_00779. |
KEGGi | sauf:X998_0910. |
PATRICi | fig|1280.10758.peg.803. |
Similar proteinsi
Entry informationi
Entry namei | X5EMW7_STAAU | |
Accessioni | X5EMW7Primary (citable) accession number: X5EMW7 | |
Entry historyi | Integrated into UniProtKB/TrEMBL: | June 11, 2014 |
Last sequence update: | June 11, 2014 | |
Last modified: | March 28, 2018 | |
This is version 43 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Unreviewed (UniProtKB/TrEMBL) |
Miscellaneousi
Caution
Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation