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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

BioCyciSPYO160490:GJ81-1089-MONOMER.
SPYO293653:GHFC-1132-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: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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512D-alanine--poly(phosphoribitol) ligase subunit 1PRO_0000213165Add
BLAST

Proteomic databases

PaxDbiQ99ZA6.

Interactioni

Protein-protein interaction databases

STRINGi160490.SPy_1312.

Structurei

Secondary structure

1
512
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511Combined sources
Turni16 – 183Combined sources
Beta strandi19 – 246Combined sources
Beta strandi27 – 304Combined sources
Helixi31 – 4717Combined sources
Beta strandi56 – 605Combined sources
Helixi64 – 7512Combined sources
Beta strandi80 – 845Combined sources
Helixi89 – 9911Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi115 – 1217Combined sources
Helixi122 – 13110Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi160 – 1656Combined sources
Helixi166 – 17813Combined sources
Turni180 – 1823Combined sources
Beta strandi189 – 1913Combined sources
Helixi199 – 2013Combined sources
Helixi202 – 21110Combined sources
Beta strandi214 – 2163Combined sources
Helixi220 – 2223Combined sources
Helixi226 – 2349Combined sources
Beta strandi239 – 2435Combined sources
Helixi245 – 2517Combined sources
Turni259 – 2613Combined sources
Beta strandi267 – 2704Combined sources
Helixi277 – 28610Combined sources
Beta strandi291 – 2966Combined sources
Helixi299 – 3013Combined sources
Beta strandi305 – 3106Combined sources
Helixi312 – 3176Combined sources
Beta strandi324 – 3263Combined sources
Beta strandi332 – 3354Combined sources
Beta strandi348 – 3547Combined sources
Helixi365 – 3717Combined sources
Beta strandi372 – 3754Combined sources
Beta strandi378 – 38912Combined sources
Beta strandi395 – 4006Combined sources
Helixi401 – 4033Combined sources
Beta strandi407 – 4093Combined sources
Helixi414 – 4229Combined sources
Beta strandi427 – 43610Combined sources
Beta strandi442 – 45110Combined sources
Helixi462 – 47211Combined sources
Turni474 – 4763Combined sources
Turni479 – 4813Combined sources
Beta strandi484 – 4885Combined sources
Beta strandi498 – 5003Combined sources
Helixi502 – 5076Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LGXX-ray2.60A/B/C/D3-512[»]
ProteinModelPortaliQ99ZA6.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651D → N in AAZ51691 (PubMed:16088826).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3LGXX-ray2.60A/B/C/D3-512[»]
ProteinModelPortaliQ99ZA6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160490.SPy_1312.

Proteomic databases

PaxDbiQ99ZA6.

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.
BioCyciSPYO160490:GJ81-1089-MONOMER.
SPYO293653:GHFC-1132-MONOMER.

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: September 7, 2016
This is version 96 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.