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Protein

D-alanine--D-alanyl carrier protein ligase

Gene

dltA

Organism
Streptococcus pyogenes serotype M1
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 sitei199D-alanineUniRule annotation1
Binding sitei303D-alanine; via carbonyl oxygenUniRule annotation1
Binding sitei385ATPUniRule annotationCombined sources1 Publication1
Binding sitei499ATPUniRule annotationCombined sources1 Publication1
Binding sitei499D-alanineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi152 – 153ATPUniRule annotationCombined sources1 Publication2
Nucleotide bindingi294 – 299ATPUniRule annotationCombined sources1 Publication6
Nucleotide bindingi397 – 400ATPUniRule annotationCombined sources1 Publication4

GO - Molecular functioni

GO - Biological processi

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:SPy_1312, M5005_Spy1073
OrganismiStreptococcus pyogenes serotype M1
Taxonomic identifieri301447 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000750 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002131651 – 512D-alanine--D-alanyl carrier protein ligaseAdd BLAST512

Proteomic databases

PaxDbiQ99ZA6
PRIDEiQ99ZA6

Interactioni

Protein-protein interaction databases

STRINGi160490.SPy_1312

Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 15Combined sources11
Turni16 – 18Combined sources3
Beta strandi19 – 24Combined sources6
Beta strandi27 – 30Combined sources4
Helixi31 – 47Combined sources17
Beta strandi56 – 60Combined sources5
Helixi64 – 75Combined sources12
Beta strandi80 – 84Combined sources5
Helixi89 – 99Combined sources11
Beta strandi102 – 108Combined sources7
Beta strandi115 – 121Combined sources7
Helixi122 – 131Combined sources10
Beta strandi145 – 152Combined sources8
Beta strandi160 – 165Combined sources6
Helixi166 – 178Combined sources13
Turni180 – 182Combined sources3
Beta strandi189 – 191Combined sources3
Helixi199 – 201Combined sources3
Helixi202 – 211Combined sources10
Beta strandi214 – 216Combined sources3
Helixi220 – 222Combined sources3
Helixi226 – 234Combined sources9
Beta strandi239 – 243Combined sources5
Helixi245 – 251Combined sources7
Turni259 – 261Combined sources3
Beta strandi267 – 270Combined sources4
Helixi277 – 286Combined sources10
Beta strandi291 – 296Combined sources6
Helixi299 – 301Combined sources3
Beta strandi305 – 310Combined sources6
Helixi312 – 317Combined sources6
Beta strandi324 – 326Combined sources3
Beta strandi332 – 335Combined sources4
Beta strandi348 – 354Combined sources7
Helixi365 – 371Combined sources7
Beta strandi372 – 375Combined sources4
Beta strandi378 – 389Combined sources12
Beta strandi395 – 400Combined sources6
Helixi401 – 403Combined sources3
Beta strandi407 – 409Combined sources3
Helixi414 – 422Combined sources9
Beta strandi427 – 436Combined sources10
Beta strandi442 – 451Combined sources10
Helixi462 – 472Combined sources11
Turni474 – 476Combined sources3
Turni479 – 481Combined sources3
Beta strandi484 – 488Combined sources5
Beta strandi498 – 500Combined sources3
Helixi502 – 507Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LGXX-ray2.60A/B/C/D3-512[»]
ProteinModelPortaliQ99ZA6
SMRiQ99ZA6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99ZA6

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
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.

Q99ZA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKDMIDSIE QFAQTQADFP VYDCLGERRT YGQLKRDSDS IAAFIDSLAL
60 70 80 90 100
LAKSPVLVFG AQTYDMLATF VALTKSGHAY IPVDVHSAPE RILAIIEIAK
110 120 130 140 150
PSLIIAIEEF PLTIEGISLV SLSEIESAKL AEMPYERTHS VKGDDNYYII
160 170 180 190 200
FTSGTTGQPK GVQISHDNLL SFTNWMIEDA AFDVPKQPQM LAQPPYSFDL
210 220 230 240 250
SVMYWAPTLA LGGTLFALPK ELVADFKQLF TTIAQLPVGI WTSTPSFADM
260 270 280 290 300
AMLSDDFCQA KMPALTHFYF DGEELTVSTA RKLFERFPSA KIINAYGPTE
310 320 330 340 350
ATVALSAIEI TREMVDNYTR LPIGYPKPDS PTYIIDEDGK ELSSGEQGEI
360 370 380 390 400
IVTGPAVSKG YLNNPEKTAE AFFTFKGQPA YHTGDIGSLT EDNILLYGGR
410 420 430 440 450
LDFQIKYAGY RIELEDVSQQ LNQSPMVASA VAVPRYNKEH KVQNLLAYIV
460 470 480 490 500
VKDGVKERFD RELELTKAIK ASVKDHMMSY MMPSKFLYRD SLPLTPNGKI
510
DIKTLINEVN NR
Length:512
Mass (Da):56,987
Last modified:June 1, 2001 - v1
Checksum:i330928DC894A6146
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti65D → N in AAZ51691 (PubMed:16088826).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA Translation: AAK34156.1
CP000017 Genomic DNA Translation: AAZ51691.1
RefSeqiNP_269435.1, NC_002737.2

Genome annotation databases

EnsemblBacteriaiAAK34156; AAK34156; SPy_1312
AAZ51691; AAZ51691; M5005_Spy1073
GeneIDi901401
KEGGispy:SPy_1312
spz:M5005_Spy1073
PATRICifig|160490.10.peg.1149

Similar proteinsi

Entry informationi

Entry nameiDLTA_STRP1
AccessioniPrimary (citable) accession number: Q99ZA6
Secondary accession number(s): Q48Y81
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2001
Last modified: March 28, 2018
This is version 102 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

3D-structure, Complete proteome, Reference proteome

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