Q1ELU4 · LAT4B_LACTA
- ProteinM-zodatoxin-Lt4b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids179 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
M-zodatoxin-Lt4b: Has antimicrobial activity against Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC=0.3 uM), and B.subtilis VKM B-501 (MIC=1.1 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=4.4 uM), E.coli MH1 (MIC=4.4 uM), and P.aeruginosa PAO1 (MIC=>35 uM)), and yeasts (P.pastoris GS115 (MIC=>35 uM), and S.cerevisiae Y190 (MIC=35 uM)). Does not have hemolytic activity against rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (M.domestica) larvae.
Repetitive polypeptide element type 1c
Shows no antimicrobial activity against Gram-positive bacterium B.subtilis B-501 or Gram-negative bacterium E.coli DH5-alpha at concentration up to 20 uM.
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 | extracellular region | |
Molecular Function | toxin activity | |
Biological Process | defense response to bacterium | |
Biological Process | defense response to fungus | |
Biological Process | killing of cells of another organism |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameM-zodatoxin-Lt4b
- Short namesM-ZDTX-Lt4b
- Cleaved into 3 chains
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Araneae > Araneomorphae > Entelegynae > Entelegynae incertae sedis > Zodariidae > Lachesana
Accessions
- Primary accessionQ1ELU4
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, peptide, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MKFSIIALALAVAFVCVAESRS | ||||||
Propeptide | PRO_0000249746 | 23-43 | ||||
Sequence: EEEGYDVSEEIQAEELEEAAR | ||||||
Peptide | PRO_0000434688 | 44-61 | Repetitive polypeptide element type 1c | |||
Sequence: GGINRKLMEMVNKLRKVQ | ||||||
Modified residue | 61 | Glutamine amide | ||||
Sequence: Q | ||||||
Propeptide | PRO_0000434689 | 63-71 | ||||
Sequence: REDSEDAGR | ||||||
Peptide | PRO_0000434690 | 72-89 | Repetitive polypeptide element type 1d | |||
Sequence: AGINRKLMEMVNKLRKVQ | ||||||
Modified residue | 89 | Glutamine amide | ||||
Sequence: Q | ||||||
Propeptide | PRO_0000434691 | 91-99 | ||||
Sequence: REDTEEAGR | ||||||
Peptide | PRO_0000434692 | 100-117 | Repetitive polypeptide element type 1c | |||
Sequence: GGINRKLMEMVNKLRKVQ | ||||||
Modified residue | 117 | Glutamine amide | ||||
Sequence: Q | ||||||
Propeptide | PRO_0000434693 | 119-127 | ||||
Sequence: REDSEEAGR | ||||||
Peptide | PRO_0000434694 | 128-145 | Repetitive polypeptide element type 1c | |||
Sequence: GGINRKLMEMVNKLRKVQ | ||||||
Modified residue | 145 | Glutamine amide | ||||
Sequence: Q | ||||||
Propeptide | PRO_0000434695 | 147-154 | ||||
Sequence: REDTEEAR | ||||||
Peptide | PRO_0000249747 | 155-178 | M-zodatoxin-Lt4b peptide | |||
Sequence: SLKDKVKSMGEKLKQYIQTWKAKF | ||||||
Modified residue | 178 | Phenylalanine amide | ||||
Sequence: F |
Post-translational modification
Cleavage of the propeptide depends on the processing quadruplet motif (PQM) (XXXR, with at least one of X being E) and the inverted PQM (RXXX, with at least one of X being E).
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 40-43 | Processing quadruplet motif 1 | ||||
Sequence: EAAR | ||||||
Motif | 63-66 | Inverted processing quadruplet motif 1 | ||||
Sequence: REDS | ||||||
Motif | 68-71 | Processing quadruplet motif 2 | ||||
Sequence: DAGR | ||||||
Motif | 91-94 | Inverted processing quadruplet motif 2 | ||||
Sequence: REDT | ||||||
Motif | 96-99 | Processing quadruplet motif 3 | ||||
Sequence: EAGR | ||||||
Motif | 119-122 | Inverted processing quadruplet motif 3 | ||||
Sequence: REDS | ||||||
Motif | 124-127 | Processing quadruplet motif 4 | ||||
Sequence: EAGR | ||||||
Motif | 147-150 | Inverted processing quadruplet motif 4 | ||||
Sequence: REDT | ||||||
Motif | 151-154 | Processing quadruplet motif 5 | ||||
Sequence: EEAR |
Domain
M-zodatoxin-Lt4a: Probably forms an alpha-helix which disrupts target cell membranes.
Sequence similarities
Belongs to the cationic peptide 03 (latarcin) family. 04 subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length179
- Mass (Da)20,364
- Last updated2006-07-11 v1
- ChecksumA6D4CFDD58A437C7
Mass Spectrometry
M-zodatoxin-Lt4b peptide
Molecular mass is 2,882.3 Da. Determined by MALDI. M-zodatoxin-Lt4b peptide.M-zodatoxin-Lt4b peptide
Molecular mass is 2,884.7 Da. Determined by MALDI. M-zodatoxin-Lt4b peptide.Repetitive polypeptide element type 1c
Molecular mass is 2,113.6 Da. Determined by MALDI. Repetitive polypeptide element type 1c.Keywords
- Technical term