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Protein

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

Gene

dltA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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.

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

BioCyciBSUB:BSU38500-MONOMER.
BRENDAi6.1.1.13. 658.
SABIO-RKP39581.
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
Synonyms:dae
Ordered Locus Names:BSU38500
ORF Names:ipa-5r
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002131421 – 503D-alanine--poly(phosphoribitol) ligase subunit 1Add BLAST503

Proteomic databases

PaxDbiP39581.
PRIDEiP39581.

Interactioni

Protein-protein interaction databases

IntActiP39581. 1 interactor.
MINTiMINT-8366705.
STRINGi224308.Bsubs1_010100020786.

Structurei

Secondary structure

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 13Combined sources11
Beta strandi17 – 22Combined sources6
Beta strandi25 – 28Combined sources4
Helixi29 – 43Combined sources15
Turni44 – 46Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi55 – 61Combined sources7
Helixi63 – 75Combined sources13
Beta strandi79 – 83Combined sources5
Helixi88 – 98Combined sources11
Beta strandi102 – 108Combined sources7
Beta strandi120 – 122Combined sources3
Helixi123 – 127Combined sources5
Helixi136 – 138Combined sources3
Beta strandi144 – 151Combined sources8
Beta strandi159 – 164Combined sources6
Helixi165 – 178Combined sources14
Turni180 – 184Combined sources5
Beta strandi186 – 189Combined sources4
Helixi197 – 207Combined sources11
Beta strandi211 – 214Combined sources4
Helixi217 – 221Combined sources5
Helixi223 – 233Combined sources11
Beta strandi236 – 240Combined sources5
Helixi242 – 249Combined sources8
Turni256 – 258Combined sources3
Beta strandi264 – 267Combined sources4
Helixi274 – 283Combined sources10
Beta strandi288 – 291Combined sources4
Helixi296 – 298Combined sources3
Beta strandi302 – 307Combined sources6
Helixi309 – 312Combined sources4
Beta strandi321 – 323Combined sources3
Beta strandi328 – 332Combined sources5
Beta strandi345 – 351Combined sources7
Helixi362 – 368Combined sources7
Beta strandi369 – 387Combined sources19
Beta strandi390 – 403Combined sources14
Beta strandi406 – 409Combined sources4
Helixi410 – 419Combined sources10
Beta strandi423 – 431Combined sources9
Beta strandi433 – 436Combined sources4
Beta strandi439 – 446Combined sources8
Helixi454 – 468Combined sources15
Helixi471 – 473Combined sources3
Beta strandi476 – 480Combined sources5
Helixi488 – 490Combined sources3
Helixi494 – 503Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E7WX-ray2.28A1-503[»]
3E7XX-ray2.60A1-503[»]
ProteinModelPortaliP39581.
SMRiP39581.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39581.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family. DltA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IQD. Bacteria.
COG1020. LUCA.
HOGENOMiHOG000229995.
InParanoidiP39581.
KOiK03367.
OMAiPIARQTM.
PhylomeDBiP39581.

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.

P39581-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLHAIQTH AETYPQTDAF RSQGQSLTYQ ELWEQSDRAA AAIQKRISGE
60 70 80 90 100
KKSPILVYGH MEPHMIVSFL GSVKAGHPYI PVDLSIPSER IAKIIESSGA
110 120 130 140 150
ELLIHAAGLS IDAVGQQIQT VSAEELLENE GGSVSQDQWV KEHETFYIIY
160 170 180 190 200
TSGSTGNPKG VQISAANLQS FTDWICADFP VSGGKIFLNQ APFSFDLSVM
210 220 230 240 250
DLYPCLQSGG TLHCVTKDAV NKPKVLFEEL KKSGLNVWTS TPSFVQMCLM
260 270 280 290 300
DPGFSQDLLP HADTFMFCGE VLPVSVAKAL LERFPKAKIF NTYGPTEATV
310 320 330 340 350
AVTSVEITND VISRSESLPV GFAKPDMNIF IMDEEGQPLP EGEKGEIVIA
360 370 380 390 400
GPSVSRGYLG EPELTEKAFF SHEGQWAYRT GDAGFIQDGQ IFCQGRLDFQ
410 420 430 440 450
IKLHGYRMEL EEIEFHVRQS QYVRSAVVIP YQPNGTVEYL IAAIVPEEHE
460 470 480 490 500
FEKEFQLTSA IKKELAASLP AYMIPRKFIY QDHIQMTANG KIDRKRIGEE

VLV
Length:503
Mass (Da):55,809
Last modified:February 1, 1995 - v1
Checksum:i76604AA90C812644
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51561.1.
AL009126 Genomic DNA. Translation: CAB15876.1.
PIRiS39660.
RefSeqiNP_391729.1. NC_000964.3.
WP_003242511.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15876; CAB15876; BSU38500.
GeneIDi937358.
KEGGibsu:BSU38500.
PATRICi18979748. VBIBacSub10457_4036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51561.1.
AL009126 Genomic DNA. Translation: CAB15876.1.
PIRiS39660.
RefSeqiNP_391729.1. NC_000964.3.
WP_003242511.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3E7WX-ray2.28A1-503[»]
3E7XX-ray2.60A1-503[»]
ProteinModelPortaliP39581.
SMRiP39581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP39581. 1 interactor.
MINTiMINT-8366705.
STRINGi224308.Bsubs1_010100020786.

Proteomic databases

PaxDbiP39581.
PRIDEiP39581.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15876; CAB15876; BSU38500.
GeneIDi937358.
KEGGibsu:BSU38500.
PATRICi18979748. VBIBacSub10457_4036.

Phylogenomic databases

eggNOGiENOG4108IQD. Bacteria.
COG1020. LUCA.
HOGENOMiHOG000229995.
InParanoidiP39581.
KOiK03367.
OMAiPIARQTM.
PhylomeDBiP39581.

Enzyme and pathway databases

UniPathwayiUPA00556.
BioCyciBSUB:BSU38500-MONOMER.
BRENDAi6.1.1.13. 658.
SABIO-RKP39581.

Miscellaneous databases

EvolutionaryTraceiP39581.

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_BACSU
AccessioniPrimary (citable) accession number: P39581
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 118 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.