Q9R9J0 (MYCB_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 53.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Mycosubtilin synthase subunit B EC=2.3.1.- Including the following 4 domains:
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| Gene names |
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| Organism | Bacillus subtilis | ||
| Taxonomic identifier | 1423 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 5369 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr, Asn, Gln and Pro as part of the synthesis of mycosubtilin. The Asn and Gln residues are further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. |
| Cofactor | Binds 4 phosphopantetheines covalently Potential. |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. Contains 4 acyl carrier domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic biosynthesis |
| Domain | Repeat |
| Ligand | Phosphopantetheine |
| Molecular function | Transferase |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor bindingInferred from electronic annotation. Source: InterPro ligase activityInferred from electronic annotation. Source: InterPro phosphopantetheine bindingInferred from electronic annotation. Source: InterPro transferase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 5369 | 5369 | Mycosubtilin synthase subunit B | PRO_0000360849 | |||||
Regions | |||||||||
| Domain | 769 – 835 | 67 | Acyl carrier 1 | ||||||
| Domain | 2280 – 2346 | 67 | Acyl carrier 2 | ||||||
| Domain | 3806 – 3873 | 68 | Acyl carrier 3 | ||||||
| Domain | 4845 – 4912 | 68 | Acyl carrier 4 | ||||||
| Region | 260 – 1620 | 1361 | Domain 1 (D-tyrosine-activating) | ||||||
| Region | 290 – 686 | 397 | Adenylation 1 | ||||||
| Region | 846 – 1305 | 460 | Epimerization 1 | ||||||
| Region | 1315 – 1615 | 301 | Condensation 1 | ||||||
| Region | 1770 – 3132 | 1363 | Domain 2 (D-asparagine-activating) | ||||||
| Region | 1800 – 2197 | 398 | Adenylation 2 | ||||||
| Region | 2357 – 2816 | 460 | Epimerization 2 | ||||||
| Region | 2826 – 3127 | 302 | Condensation 2 | ||||||
| Region | 3281 – 4182 | 902 | Domain 3 (glutamine-activating) | ||||||
| Region | 3311 – 3723 | 413 | Adenylation 3 | ||||||
| Region | 3888 – 4177 | 290 | Condensation 3 | ||||||
| Region | 4334 – 5221 | 888 | Domain 4 (proline-activating) | ||||||
| Region | 4364 – 4762 | 399 | Adenylation 4 | ||||||
| Region | 4927 – 5216 | 290 | Condensation 4 | ||||||
| Compositional bias | 101 – 104 | 4 | Poly-Ser | ||||||
Amino acid modifications | |||||||||
| Modified residue | 799 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 2310 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 3836 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 4875 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
Sequences
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References
| [1] | "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a multifunctional hybrid between a peptide synthetase, an amino transferase, and a fatty acid synthase." Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W., Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F., Vater J. Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999) [PubMed: 10557314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 6633 / PCI 219 / NRS 231. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF184956 Genomic DNA. Translation: AAF08796.1. |
| PIR | T44807. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DNY based on UniProtKB O30409. |
| ProteinModelPortal | Q9R9J0. |
| SMR | Q9R9J0. Positions 3797-4313. |
| 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. IPR006162. PPantetheine_attach_site. [Graphical view] |
| Gene3D | G3DSA:1.10.1200.10. ACP_like. 4 hits. |
| Pfam | PF00501. AMP-binding. 4 hits. PF00668. Condensation. 7 hits. PF00550. PP-binding. 4 hits. [Graphical view] |
| SUPFAM | SSF47336. ACP_like. 4 hits. |
| TIGRFAMs | TIGR01733. AA-adenyl-dom. 4 hits. TIGR01720. NRPS-para261. 2 hits. |
| PROSITE | PS50075. ACP_DOMAIN. 4 hits. PS00455. AMP_BINDING. 3 hits. PS00012. PHOSPHOPANTETHEINE. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MYCB_BACSU | ||||||||
| Accession | Primary (citable) accession number: Q9R9J0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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