P0C8P7 · THCL_BACBA
- ProteinThiocillin
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Has bacteriocidal activity against Gram-positive bacteria, but not against Gram-negative bacteria. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 6 | Not hydroxylated; in form thiocillin III | ||||
Sequence: V |
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 | |
Biological Process | defense response to bacterium | |
Biological Process | killing of cells of another organism |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameThiocillin
Organism names
- Organism
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP0C8P7
Subcellular Location
PTM/Processing
Features
Showing features for cross-link, peptide, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Cross-link | 1↔2 | Thiazole-4-carboxylic acid (Ser-Cys) | ||||
Sequence: SC | ||||||
Cross-link | 1↔9 | Pyridine-2,5-dicarboxylic acid (Ser-Cys) (with S-10) | ||||
Sequence: SCTTCVCTC | ||||||
Cross-link | 1↔10 | Pyridine-2,5-dicarboxylic acid (Ser-Ser) (with C-9) | ||||
Sequence: SCTTCVCTCS | ||||||
Peptide | PRO_0000363168 | 1-14 | Thiocillin | |||
Sequence: SCTTCVCTCSCCTT | ||||||
Modified residue | 4 | (Z)-2,3-didehydrobutyrine | ||||
Sequence: T | ||||||
Cross-link | 4↔5 | Thiazole-4-carboxylic acid (Thr-Cys) | ||||
Sequence: TC | ||||||
Modified residue | 6 | 3-hydroxyvaline (Val); in form thiocillin II | ||||
Sequence: V | ||||||
Cross-link | 6↔7 | Thiazole-4-carboxylic acid (Val-Cys) | ||||
Sequence: VC | ||||||
Modified residue | 8 | O-methylthreonine; in form thiocillin II and form thiocillin III | ||||
Sequence: T | ||||||
Cross-link | 8↔9 | Thiazole-4-carboxylic acid (Thr-Cys) | ||||
Sequence: TC | ||||||
Cross-link | 10↔11 | Thiazole-4-carboxylic acid (Ser-Cys) | ||||
Sequence: SC | ||||||
Cross-link | 11↔12 | Thiazole-4-carboxylic acid (Cys-Cys) | ||||
Sequence: CC | ||||||
Modified residue | 13 | (Z)-2,3-didehydrobutyrine | ||||
Sequence: T | ||||||
Modified residue | 14 | Decarboxylated threonine | ||||
Sequence: T |
Post-translational modification
Maturation of thiazole and oxazole containing antibiotics involves the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogenated to form thiazole or oxazole rings.
Maturation of pyridinyl containing antibiotics involves the cross-linking of a Ser and a Cys-Ser pair usually separated by 7 or 8 residues along the peptide chain. The Ser residues are dehydrated to didehydroalanines, then bonded between their beta carbons. The alpha carbonyl of the Cys condenses with alpha carbon of the first Ser to form a pyridinyl ring. The ring may be multiply dehydrogenated to form a pyridine ring with loss of the amino nitrogen of the first Ser.
3 isomers may exist: thiocillin I, identified in B.cereus G-15, thiocillin II, identified in both B.badius and B.cereus G-15, and thiocillin III identified in B.badius only. The structural differences between them lie in the extent of the modifications at two positions, as shown in the feature table.
The structure of the 2,3-didehydrobutyrines is not discussed in PubMed:7328054. However, in Fig. 1 the residues are diagrammed as Z-isomers.
Keywords
- PTM