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Protein

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

Gene

dltA

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
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

BRENDAi6.1.1.13. 648.
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:BC_1372
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001417 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_10000255261 – 504D-alanine--poly(phosphoribitol) ligase subunit 1Add BLAST504

Proteomic databases

PRIDEiQ81G39.

Interactioni

Protein-protein interaction databases

STRINGi226900.BC1372.

Structurei

Secondary structure

1504
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 – 46Combined sources18
Beta strandi54 – 60Combined sources7
Helixi62 – 73Combined sources12
Beta strandi78 – 82Combined sources5
Helixi87 – 96Combined sources10
Beta strandi101 – 106Combined sources6
Beta strandi114 – 119Combined sources6
Helixi121 – 129Combined sources9
Turni130 – 132Combined sources3
Helixi137 – 139Combined sources3
Beta strandi145 – 152Combined sources8
Beta strandi160 – 165Combined sources6
Helixi166 – 179Combined sources14
Beta strandi187 – 190Combined sources4
Helixi197 – 199Combined sources3
Helixi200 – 208Combined sources9
Beta strandi212 – 215Combined sources4
Helixi218 – 222Combined sources5
Helixi224 – 234Combined sources11
Beta strandi238 – 241Combined sources4
Helixi243 – 249Combined sources7
Turni257 – 259Combined sources3
Beta strandi265 – 268Combined sources4
Helixi275 – 284Combined sources10
Beta strandi289 – 294Combined sources6
Helixi297 – 299Combined sources3
Beta strandi303 – 307Combined sources5
Helixi310 – 315Combined sources6
Beta strandi322 – 324Combined sources3
Beta strandi329 – 333Combined sources5
Beta strandi335 – 337Combined sources3
Beta strandi346 – 352Combined sources7
Helixi363 – 369Combined sources7
Beta strandi370 – 373Combined sources4
Beta strandi376 – 388Combined sources13
Beta strandi391 – 397Combined sources7
Helixi398 – 400Combined sources3
Beta strandi402 – 404Combined sources3
Beta strandi407 – 409Combined sources3
Helixi411 – 420Combined sources10
Beta strandi424 – 434Combined sources11
Beta strandi437 – 447Combined sources11
Helixi455 – 467Combined sources13
Helixi472 – 474Combined sources3
Beta strandi477 – 481Combined sources5
Beta strandi491 – 493Combined sources3
Helixi495 – 503Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DHVX-ray2.00A1-504[»]
3FCCX-ray2.32A1-504[»]
3FCEX-ray1.90A1-504[»]
4PZPX-ray1.90A2-504[»]
ProteinModelPortaliQ81G39.
SMRiQ81G39.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81G39.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQD. Bacteria.
COG1020. LUCA.
KOiK03367.
OMAiTHKGKTP.

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.

Q81G39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLEQIEKW AAETPDQTAF VWRDAKITYK QLKEDSDALA HWISSEYPDD
60 70 80 90 100
RSPIMVYGHM QPEMIINFLG CVKAGHAYIP VDLSIPADRV QRIAENSGAK
110 120 130 140 150
LLLSATAVTV TDLPVRIVSE DNLKDIFFTH KGNTPNPEHA VKGDENFYII
160 170 180 190 200
YTSGSTGNPK GVQITYNCLV SFTKWAVEDF NLQTGQVFLN QAPFSFDLSV
210 220 230 240 250
MDIYPSLVTG GTLWAIDKDM IARPKDLFAS LEQSDIQVWT STPSFAEMCL
260 270 280 290 300
MEASFSESML PNMKTFLFCG EVLPNEVARK LIERFPKATI MNTYGPTEAT
310 320 330 340 350
VAVTGIHVTE EVLDQYKSLP VGYCKSDCRL LIMKEDGTIA PDGEKGEIVI
360 370 380 390 400
VGPSVSVGYL GSPELTEKAF TMIDGERAYK TGDAGYVENG LLFYNGRLDF
410 420 430 440 450
QIKLHGYRME LEEIEHHLRA CSYVEGAVIV PIKKGEKYDY LLAVVVPGEH
460 470 480 490 500
SFEKEFKLTS AIKKELNERL PNYMIPRKFM YQSSIPMTPN GKVDRKKLLS

EVTA
Length:504
Mass (Da):56,494
Last modified:June 1, 2003 - v1
Checksum:i96BE762A25E315D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP08354.1.
RefSeqiNP_831153.1. NC_004722.1.
WP_000770505.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP08354; AAP08354; BC_1372.
GeneIDi1203721.
KEGGibce:BC1372.
PATRICi32598473. VBIBacCer54481_1346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP08354.1.
RefSeqiNP_831153.1. NC_004722.1.
WP_000770505.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DHVX-ray2.00A1-504[»]
3FCCX-ray2.32A1-504[»]
3FCEX-ray1.90A1-504[»]
4PZPX-ray1.90A2-504[»]
ProteinModelPortaliQ81G39.
SMRiQ81G39.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC1372.

Proteomic databases

PRIDEiQ81G39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP08354; AAP08354; BC_1372.
GeneIDi1203721.
KEGGibce:BC1372.
PATRICi32598473. VBIBacCer54481_1346.

Phylogenomic databases

eggNOGiENOG4108IQD. Bacteria.
COG1020. LUCA.
KOiK03367.
OMAiTHKGKTP.

Enzyme and pathway databases

UniPathwayiUPA00556.
BRENDAi6.1.1.13. 648.

Miscellaneous databases

EvolutionaryTraceiQ81G39.

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_BACCR
AccessioniPrimary (citable) accession number: Q81G39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 85 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.