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Q81G39

- DLTA_BACCR

UniProt

Q81G39 - DLTA_BACCR

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Protein

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

Gene
dltA, BC_1372
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate).UniRule annotation

Pathwayi

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. D-alanine-poly(phosphoribitol) ligase activity Source: UniProtKB-EC

GO - Biological processi

  1. lipoteichoic acid biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBCER226900:GJEU-1372-MONOMER.
UniPathwayiUPA00556.

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanine--poly(phosphoribitol) ligase subunit 1 (EC:6.1.1.13)
Alternative name(s):
D-alanine-D-alanyl carrier protein ligase
Short name:
DCL
D-alanine-activating enzyme
Short name:
DAE
Gene namesi
Name:dltA
Ordered Locus Names:BC_1372
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504D-alanine--poly(phosphoribitol) ligase subunit 1UniRule annotationPRO_1000025526Add
BLAST

Proteomic databases

PRIDEiQ81G39.

Interactioni

Protein-protein interaction databases

STRINGi226900.BC1372.

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311
Beta strandi17 – 226
Beta strandi25 – 284
Helixi29 – 4618
Beta strandi54 – 607
Helixi62 – 7312
Beta strandi78 – 825
Helixi87 – 9610
Beta strandi101 – 1066
Beta strandi114 – 1196
Helixi121 – 1299
Turni130 – 1323
Helixi137 – 1393
Beta strandi145 – 1528
Beta strandi160 – 1656
Helixi166 – 17914
Beta strandi187 – 1904
Helixi197 – 1993
Helixi200 – 2089
Beta strandi212 – 2154
Helixi218 – 2225
Helixi224 – 23411
Beta strandi238 – 2414
Helixi243 – 2497
Turni257 – 2593
Beta strandi265 – 2684
Helixi275 – 28410
Beta strandi289 – 2946
Helixi297 – 2993
Beta strandi303 – 3075
Helixi310 – 3156
Beta strandi322 – 3243
Beta strandi329 – 3335
Beta strandi335 – 3373
Beta strandi346 – 3527
Helixi363 – 3697
Beta strandi370 – 3734
Beta strandi376 – 38813
Beta strandi391 – 3977
Helixi398 – 4003
Beta strandi402 – 4043
Beta strandi407 – 4093
Helixi411 – 42010
Beta strandi424 – 43411
Beta strandi437 – 44711
Helixi455 – 46713
Helixi472 – 4743
Beta strandi477 – 4815
Beta strandi491 – 4933
Helixi495 – 5039

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DHVX-ray2.00A1-504[»]
3FCCX-ray2.32A1-504[»]
3FCEX-ray1.90A1-504[»]
ProteinModelPortaliQ81G39.

Miscellaneous databases

EvolutionaryTraceiQ81G39.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1020.
KOiK03367.
OMAiIANQAPF.
OrthoDBiEOG6QP0WP.

Family and domain databases

HAMAPiMF_00593. DltA.
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

MKLLEQIEKW AAETPDQTAF VWRDAKITYK QLKEDSDALA HWISSEYPDD    50
RSPIMVYGHM QPEMIINFLG CVKAGHAYIP VDLSIPADRV QRIAENSGAK 100
LLLSATAVTV TDLPVRIVSE DNLKDIFFTH KGNTPNPEHA VKGDENFYII 150
YTSGSTGNPK GVQITYNCLV SFTKWAVEDF NLQTGQVFLN QAPFSFDLSV 200
MDIYPSLVTG GTLWAIDKDM IARPKDLFAS LEQSDIQVWT STPSFAEMCL 250
MEASFSESML PNMKTFLFCG EVLPNEVARK LIERFPKATI MNTYGPTEAT 300
VAVTGIHVTE EVLDQYKSLP VGYCKSDCRL LIMKEDGTIA PDGEKGEIVI 350
VGPSVSVGYL GSPELTEKAF TMIDGERAYK TGDAGYVENG LLFYNGRLDF 400
QIKLHGYRME LEEIEHHLRA CSYVEGAVIV PIKKGEKYDY LLAVVVPGEH 450
SFEKEFKLTS AIKKELNERL PNYMIPRKFM YQSSIPMTPN GKVDRKKLLS 500
EVTA 504
Length:504
Mass (Da):56,494
Last modified:June 1, 2003 - v1
Checksum:i96BE762A25E315D2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016877 Genomic DNA. Translation: AAP08354.1.
RefSeqiNP_831153.1. NC_004722.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016877 Genomic DNA. Translation: AAP08354.1 .
RefSeqi NP_831153.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DHV X-ray 2.00 A 1-504 [» ]
3FCC X-ray 2.32 A 1-504 [» ]
3FCE X-ray 1.90 A 1-504 [» ]
ProteinModelPortali Q81G39.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 226900.BC1372.

Proteomic databases

PRIDEi Q81G39.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP08354 ; AAP08354 ; BC_1372 .
GeneIDi 1203721.
KEGGi bce:BC1372.
PATRICi 32598473. VBIBacCer54481_1346.

Phylogenomic databases

eggNOGi COG1020.
KOi K03367.
OMAi IANQAPF.
OrthoDBi EOG6QP0WP.

Enzyme and pathway databases

UniPathwayi UPA00556 .
BioCyci BCER226900:GJEU-1372-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q81G39.

Family and domain databases

HAMAPi MF_00593. DltA.
InterProi IPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. DltA.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01733. AA-adenyl-dom. 1 hit.
TIGR01734. D-ala-DACP-lig. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31.

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: September 3, 2014
This is version 74 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

External Data

Dasty 3

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