P0ADA3 · NLPD_ECOLI
- ProteinMurein hydrolase activator NlpD
- GenenlpD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids379 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Activator of the cell wall hydrolase AmiC. Required for septal murein cleavage and daughter cell separation during cell division.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell division site | |
Cellular Component | cell outer membrane | |
Cellular Component | plasma membrane | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | cell division | |
Biological Process | response to xenobiotic stimulus |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMurein hydrolase activator NlpD
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0ADA3
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Lipid-anchor
Note: Localizes at the septal ring.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Cells are shorter in a single mutant, double envC-nlpD disruptions have defects in septation and cell separation and form long filaments (8-fold longer). Cell length increase is more exacerbated with a triple mepM (yebA) or ygeR disruption (15-fold longer) and further yet by the quadruple disruption mutant (envC-nlpD-mepM(yebA)-ygeR, over 21-fold longer). Quadruple mutants are less sensitive to ampicillin lysis.
PTM/Processing
Features
Showing features for signal, lipidation, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MSAGSPKFTVRRIAALSLVSLWLAG | ||||||
Lipidation | 26 | N-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 26 | S-diacylglycerol cysteine | ||||
Sequence: C | ||||||
Chain | PRO_0000018029 | 26-379 | Murein hydrolase activator NlpD | |||
Sequence: CSDTSNPPAPVSSVNGNAPANTNSGMLITPPPKMGTTSTAQQPQIQPVQQPQIQATQQPQIQPVQPVAQQPVQMENGRIVYNRQYGNIPKGSYSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQVGNASGTPITGGNAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPTATTVTAPVTVPTASTTEPTVSSTSTSTPISTWRWPTEGKVIETFGASEGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRYLPQR |
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Features
Showing features for region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 30-67 | Disordered | ||||
Sequence: SNPPAPVSSVNGNAPANTNSGMLITPPPKMGTTSTAQQ | ||||||
Repeat | 66-73 | 1-1 | ||||
Sequence: QQPQIQPV | ||||||
Region | 66-97 | 4 X 8 AA tandem repeats of Q-Q-P-Q-I-Q-P-V | ||||
Sequence: QQPQIQPVQQPQIQATQQPQIQPVQPVAQQPV | ||||||
Repeat | 74-81 | 1-2; approximate | ||||
Sequence: QQPQIQAT | ||||||
Repeat | 82-89 | 1-3 | ||||
Sequence: QQPQIQPV | ||||||
Repeat | 90-97 | 1-4; approximate | ||||
Sequence: QPVAQQPV | ||||||
Domain | 121-165 | LysM | ||||
Sequence: STYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQV | ||||||
Repeat | 205-211 | 2-1 | ||||
Sequence: PTITYSE | ||||||
Region | 205-252 | 4 X 7 AA approximate repeats | ||||
Sequence: PTITYSESSGEQSANKMLPNNKPTATTVTAPVTVPTASTTEPTVSSTS | ||||||
Region | 210-231 | Disordered | ||||
Sequence: SESSGEQSANKMLPNNKPTATT | ||||||
Repeat | 227-233 | 2-2 | ||||
Sequence: PTATTVT | ||||||
Repeat | 239-245 | 2-3 | ||||
Sequence: PTASTTE | ||||||
Region | 240-259 | Disordered | ||||
Sequence: TASTTEPTVSSTSTSTPIST | ||||||
Repeat | 246-252 | 2-4 | ||||
Sequence: PTVSSTS |
Sequence similarities
Belongs to the E.coli NlpD/Haemophilus LppB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length379
- Mass (Da)40,149
- Last updated2005-12-06 v1
- ChecksumA8E6A2B8456105FE
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 139 | in Ref. 4; BAA04487 | ||||
Sequence: G → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L07869 EMBL· GenBank· DDBJ | AAA17875.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
U29579 EMBL· GenBank· DDBJ | AAA69252.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC75784.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D17549 EMBL· GenBank· DDBJ | BAA04487.1 EMBL· GenBank· DDBJ | Genomic DNA |