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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

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
Status
Reviewed - 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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. 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 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)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504D-alanine--poly(phosphoribitol) ligase subunit 1PRO_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 – 1311Combined sources
Beta strandi17 – 226Combined sources
Beta strandi25 – 284Combined sources
Helixi29 – 4618Combined sources
Beta strandi54 – 607Combined sources
Helixi62 – 7312Combined sources
Beta strandi78 – 825Combined sources
Helixi87 – 9610Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi114 – 1196Combined sources
Helixi121 – 1299Combined sources
Turni130 – 1323Combined sources
Helixi137 – 1393Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi160 – 1656Combined sources
Helixi166 – 17914Combined sources
Beta strandi187 – 1904Combined sources
Helixi197 – 1993Combined sources
Helixi200 – 2089Combined sources
Beta strandi212 – 2154Combined sources
Helixi218 – 2225Combined sources
Helixi224 – 23411Combined sources
Beta strandi238 – 2414Combined sources
Helixi243 – 2497Combined sources
Turni257 – 2593Combined sources
Beta strandi265 – 2684Combined sources
Helixi275 – 28410Combined sources
Beta strandi289 – 2946Combined sources
Helixi297 – 2993Combined sources
Beta strandi303 – 3075Combined sources
Helixi310 – 3156Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi329 – 3335Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi346 – 3527Combined sources
Helixi363 – 3697Combined sources
Beta strandi370 – 3734Combined sources
Beta strandi376 – 38813Combined sources
Beta strandi391 – 3977Combined sources
Helixi398 – 4003Combined sources
Beta strandi402 – 4043Combined sources
Beta strandi407 – 4093Combined sources
Helixi411 – 42010Combined sources
Beta strandi424 – 43411Combined sources
Beta strandi437 – 44711Combined sources
Helixi455 – 46713Combined sources
Helixi472 – 4743Combined sources
Beta strandi477 – 4815Combined sources
Beta strandi491 – 4933Combined sources
Helixi495 – 5039Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ81G39.

Family & Domainsi

Sequence similaritiesi

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

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

        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.

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 .
RefSeqi NP_831153.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 77 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