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Protein

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

Gene

dltA

Organism
Streptococcus pyogenes serotype M1
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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 - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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: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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002131651 – 512D-alanine--poly(phosphoribitol) ligase subunit 1Add 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.
OMAiLFICTEE.

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.

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.
PATRICi19716169. VBIStrPyo79812_1149.

Cross-referencesi

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.

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...

Protein-protein interaction databases

STRINGi160490.SPy_1312.

Proteomic databases

PaxDbiQ99ZA6.
PRIDEiQ99ZA6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK34156; AAK34156; SPy_1312.
AAZ51691; AAZ51691; M5005_Spy1073.
GeneIDi901401.
KEGGispy:SPy_1312.
spz:M5005_Spy1073.
PATRICi19716169. VBIStrPyo79812_1149.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00556.

Miscellaneous databases

EvolutionaryTraceiQ99ZA6.

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_STRP1
AccessioniPrimary (citable) accession number: Q99ZA6
Secondary accession number(s): Q48Y81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 98 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.