UniProtKB - Q63E02 (DLTA_BACCZ)
Protein
D-alanine--D-alanyl carrier protein ligase
Gene
dltA
Organism
Bacillus cereus (strain ZK / E33L)
Status
Functioni
Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.UniRule annotation
Catalytic activityi
- ATP + D-alanine + holo-[D-alanyl-carrier protein] = AMP + D-alanyl-[D-alanyl-carrier protein] + diphosphateUniRule annotationEC:6.2.1.54UniRule annotation
: lipoteichoic acid biosynthesis Pathwayi
This protein is involved in the pathway lipoteichoic acid biosynthesis, which is part of Cell wall biogenesis.UniRule annotationView all proteins of this organism that are known to be involved in the pathway lipoteichoic acid biosynthesis and in Cell wall biogenesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 197 | D-alanineUniRule annotation | 1 | |
Binding sitei | 301 | D-alanine; via carbonyl oxygenUniRule annotation | 1 | |
Binding sitei | 383 | ATPUniRule annotation | 1 | |
Binding sitei | 492 | ATPUniRule annotation | 1 | |
Binding sitei | 492 | D-alanineUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 152 – 153 | ATPUniRule annotation | 2 | |
Nucleotide bindingi | 292 – 297 | ATPUniRule annotation | 6 | |
Nucleotide bindingi | 394 – 397 | ATPUniRule annotation | 4 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- D-alanine [D-alanyl carrier protein] ligase activity Source: UniProtKB-UniRule
GO - Biological processi
- lipoteichoic acid biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Ligase |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | BCER288681:G1G3U-1459-MONOMER |
UniPathwayi | UPA00556 |
Names & Taxonomyi
Protein namesi | Recommended name: D-alanine--D-alanyl carrier protein ligaseUniRule annotation (EC:6.2.1.54UniRule annotation)Short name: DCLUniRule annotation Alternative name(s): D-alanine--poly(phosphoribitol) ligase subunit 1UniRule annotation D-alanine-activating enzymeUniRule annotation Short name: DAEUniRule annotation |
Gene namesi | Name:dltAUniRule annotation Ordered Locus Names:BCE33L1261 |
Organismi | Bacillus cereus (strain ZK / E33L) |
Taxonomic identifieri | 288681 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_1000025527 | 1 – 504 | D-alanine--D-alanyl carrier protein ligaseAdd BLAST | 504 |
Proteomic databases
PRIDEi | Q63E02 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
KOi | K03367 |
OMAi | MDLYPCL |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
HAMAPi | MF_00593 DltA, 1 hit |
InterProi | View protein in InterPro IPR010071 AA_adenyl_domain IPR025110 AMP-bd_C IPR020845 AMP-binding_CS IPR000873 AMP-dep_Synth/Lig IPR042099 AMP-dep_Synthh-like_sf IPR010072 DltA |
Pfami | View protein in Pfam PF00501 AMP-binding, 1 hit PF13193 AMP-binding_C, 1 hit |
TIGRFAMsi | TIGR01733 AA-adenyl-dom, 1 hit TIGR01734 D-ala-DACP-lig, 1 hit |
PROSITEi | View protein in PROSITE PS00455 AMP_BINDING, 1 hit |
i Sequence
Sequence statusi: Complete.
Q63E02-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKLLEQIEKW AIETPDQTAF VWRDAKITYK QLKEDSDALA HWISSEYPDD
60 70 80 90 100
RSPIMVYGHM QPEMIINFLG CVKAGHAYIP VDLSIPADRV QRIAENSGAK
110 120 130 140 150
LLLSAATVTV TDLPVRIVSE DNLKDIFFTH KGNTPNPEHA VKGDENFYII
160 170 180 190 200
YTSGSTGNPK GVQITYNCLV SFTQWAVEDF 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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000001 Genomic DNA Translation: AAU18987.1 |
RefSeqi | WP_000770520.1, NZ_CP009968.1 |
Genome annotation databases
EnsemblBacteriai | AAU18987; AAU18987; BCE33L1261 |
KEGGi | bcz:BCE33L1261 |
PATRICi | fig|288681.22.peg.4298 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000001 Genomic DNA Translation: AAU18987.1 |
RefSeqi | WP_000770520.1, NZ_CP009968.1 |
3D structure databases
SMRi | Q63E02 |
ModBasei | Search... |
Proteomic databases
PRIDEi | Q63E02 |
Genome annotation databases
EnsemblBacteriai | AAU18987; AAU18987; BCE33L1261 |
KEGGi | bcz:BCE33L1261 |
PATRICi | fig|288681.22.peg.4298 |
Phylogenomic databases
KOi | K03367 |
OMAi | MDLYPCL |
Enzyme and pathway databases
UniPathwayi | UPA00556 |
BioCyci | BCER288681:G1G3U-1459-MONOMER |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
HAMAPi | MF_00593 DltA, 1 hit |
InterProi | View protein in InterPro IPR010071 AA_adenyl_domain IPR025110 AMP-bd_C IPR020845 AMP-binding_CS IPR000873 AMP-dep_Synth/Lig IPR042099 AMP-dep_Synthh-like_sf IPR010072 DltA |
Pfami | View protein in Pfam PF00501 AMP-binding, 1 hit PF13193 AMP-binding_C, 1 hit |
TIGRFAMsi | TIGR01733 AA-adenyl-dom, 1 hit TIGR01734 D-ala-DACP-lig, 1 hit |
PROSITEi | View protein in PROSITE PS00455 AMP_BINDING, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DLTA_BACCZ | |
Accessioni | Q63E02Primary (citable) accession number: Q63E02 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 15, 2008 |
Last sequence update: | October 25, 2004 | |
Last modified: | October 16, 2019 | |
This is version 90 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - PATHWAY comments
Index of metabolic and biosynthesis pathways