O30408 (TYCB_BREPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 72.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tyrocidine synthase 2 Alternative name(s): Tyrocidine synthase II Including the following 4 domains:
| ||
| Gene names |
| ||
| Organism | Brevibacillus parabrevis | ||
| Taxonomic identifier | 54914 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Paenibacillaceae › Brevibacillus |
Protein attributes
| Sequence length | 3587 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Activates the second to fourth amino acids in tyrocidine (in tyrocidine A, Pro, Phe, and D-Phe) and epimerizes the last one. |
| Catalytic activity | ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine. |
| Cofactor | Binds 3 phosphopantetheines covalently By similarity. |
| Pathway | |
| Subunit structure | Large multienzyme complex of TycA, TycB and TycC. |
| Domain | Consists of three modules, including a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional), and N methylation (optional). |
| Miscellaneous | Tyrocidine is a mixture of four cyclic decapeptides, tyrocidine A (D-Phe-Pro-Phe-D-Phe-Asn-Gln-Tyr-Val-Orn-Leu), B, C, and D, in which Phe, at positions 3, 4, and Tyr residues are gradually replaced by Trp, depending on the relative concentrations of these amino acids in the growth medium. |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. Contains 3 acyl carrier domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic biosynthesis |
| Domain | Repeat |
| Ligand | ATP-binding Nucleotide-binding Phosphopantetheine |
| Molecular function | Isomerase Ligase |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acyl carrier activityInferred from electronic annotation. Source: InterPro cofactor bindingInferred from electronic annotation. Source: InterPro ligase activityInferred from electronic annotation. Source: UniProtKB-KW phenylalanine racemase (ATP-hydrolyzing) activityInferred from electronic annotation. Source: EC phosphopantetheine bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 3587 | 3587 | Tyrocidine synthase 2 | PRO_0000193094 | |||||
Regions | |||||||||
| Domain | 977 – 1044 | 68 | Acyl carrier 1 | ||||||
| Domain | 2012 – 2079 | 68 | Acyl carrier 2 | ||||||
| Domain | 3045 – 3111 | 67 | Acyl carrier 3 | ||||||
| Region | 466 – 1045 | 580 | Domain 1 (Proline-activating) | ||||||
| Region | 1522 – 2081 | 560 | Domain 2 (Phenylalanine-activating) | ||||||
| Region | 2540 – 3122 | 583 | Domain 3 (D-phenylalanine-activating) | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1007 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 2042 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 3075 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The tyrocidine biosynthesis operon of Bacillus brevis: complete nucleotide sequence and biochemical characterization of functional internal adenylation domains." Mootz H.D., Marahiel M.A. J. Bacteriol. 179:6843-6850(1997) [PubMed: 9352938] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8185 / DSM 362 / JCM 20017 / NBRC 3331 / NCDO 717 / NCIMB 8598 / IAM 1031. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF004835 Genomic DNA. Translation: AAC45929.1. |
3D structure databases | |
| ProteinModelPortal | O30408. |
| SMR | O30408. Positions 967-1484, 2001-2521, 2524-3029. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR010071. AA_adenyl_domain. IPR009081. Acyl_carrier_prot-like. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR001242. Condensatn. IPR010060. NRPS_synth. IPR006163. Phsphopanteth-bd. IPR020806. PKS_PP-bd. IPR006162. PPantetheine_attach_site. [Graphical view] |
| Gene3D | G3DSA:1.10.1200.10. ACP_like. 3 hits. |
| Pfam | PF00501. AMP-binding. 3 hits. PF00668. Condensation. 4 hits. PF00550. PP-binding. 3 hits. [Graphical view] |
| SMART | SM00823. PKS_PP. 3 hits. [Graphical view] |
| SUPFAM | SSF47336. ACP_like. 3 hits. |
| TIGRFAMs | TIGR01733. AA-adenyl-dom. 3 hits. TIGR01720. NRPS-para261. 1 hit. |
| PROSITE | PS50075. ACP_DOMAIN. 3 hits. PS00455. AMP_BINDING. 3 hits. PS00012. PHOSPHOPANTETHEINE. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TYCB_BREPA | ||||||||
| Accession | Primary (citable) accession number: O30408 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |