O54329 · LANA_STRMG
- ProteinLantibiotic mutacin-2
- GenemutA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria including M.luteus, S.aureus, Streptococcus, P.micros, P.acidilactici, C.sporogenes, C.diphtheriae, A.viscosus, G.vaginalis, P.acnes, L.monocytogenes and M.smegmatis, and Gram-negative bacteria including C.jejuni, H.pylori and N.gonorrhoeae. Transiently and partially depolarizes the transmembrane electrical potential and pH gradient of susceptible cells, inhibits the uptake of amino acids and depletes the intracellular ATP pool.
pH Dependence
Stable from pH 2.0 to 4.0. Activity decreases gradually with increasing pH.
Temperature Dependence
Thermostable.
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 | signaling receptor binding | |
Biological Process | amino acid transport | |
Biological Process | defense response to Gram-negative bacterium | |
Biological Process | defense response to Gram-positive bacterium | |
Biological Process | killing of cells of another organism | |
Biological Process | regulation of membrane potential |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLantibiotic mutacin-2
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionO54329
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 14 | No loss of activity or protein production. | ||||
Sequence: E → D | ||||||
Mutagenesis | 14 | Reduced protein production to about 10% of wild-type level. | ||||
Sequence: E → K | ||||||
Mutagenesis | 15 | No loss of activity or protein production. | ||||
Sequence: V → I or A | ||||||
Mutagenesis | 15 | Reduced protein production to about 50% of wild-type level. | ||||
Sequence: V → L | ||||||
Mutagenesis | 16 | No loss of activity or protein production. | ||||
Sequence: S → T or A | ||||||
Mutagenesis | 19 | No loss of activity or protein production. | ||||
Sequence: E → D | ||||||
Mutagenesis | 19 | Reduced protein production to about 75% of wild-type level. | ||||
Sequence: E → K | ||||||
Mutagenesis | 20 | No mature protein is produced. | ||||
Sequence: L → K | ||||||
Mutagenesis | 20 | No loss of activity or protein production. | ||||
Sequence: L → M | ||||||
Mutagenesis | 23 | No mature protein is produced. | ||||
Sequence: I → D | ||||||
Mutagenesis | 23 | No loss of activity or protein production. | ||||
Sequence: I → V | ||||||
Mutagenesis | 25 | No mature protein is produced. | ||||
Sequence: G → A | ||||||
Mutagenesis | 26 | No mature protein is produced. | ||||
Sequence: G → A | ||||||
Mutagenesis | 27 | No protein is secreted. | ||||
Sequence: Missing | ||||||
Mutagenesis | 33 | No loss of activity. | ||||
Sequence: V → A | ||||||
Mutagenesis | 35 | Low activity, less than 10% of wild-type. | ||||
Sequence: P → A | ||||||
Mutagenesis | 36 | Loss of secretion. | ||||
Sequence: T → A | ||||||
Mutagenesis | 36 | No loss of activity. | ||||
Sequence: T → S | ||||||
Mutagenesis | 41 | Loss of activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 52 | Loss of activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 53 | Low activity, less than 10% of wild-type level. | ||||
Sequence: C → A |
PTM/Processing
Features
Showing features for propeptide, peptide, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000017128 | 1-26 | ||||
Sequence: MNKLNSNAVVSLNEVSDSELDTILGG | ||||||
Peptide | PRO_0000017129 | 27-53 | Lantibiotic mutacin-2 | |||
Sequence: NRWWQGVVPTVSYECRMNSWQHVFTCC | ||||||
Cross-link | 36↔41 | Beta-methyllanthionine (Thr-Cys) | ||||
Sequence: TVSYEC | ||||||
Cross-link | 38↔52 | Lanthionine (Ser-Cys) | ||||
Sequence: SYECRMNSWQHVFTC | ||||||
Cross-link | 45↔53 | Lanthionine (Ser-Cys) | ||||
Sequence: SWQHVFTCC | ||||||
Modified residue | 51 | 2,3-didehydrobutyrine | ||||
Sequence: T |
Post-translational modification
Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.
It is not established whether the 2,3-didehydrobutyrine is the E- or Z-isomer (PubMed:10821848, PubMed:16626493, PubMed:8021218, PubMed:8660519, PubMed:9647795).
Keywords
- PTM
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length53
- Mass (Da)6,020
- Last updated1998-06-01 v1
- Checksum6C3788E2C9EC6525
Mass Spectrometry
Keywords
- Technical term