O68007 (BACB_BACLI) 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: Bacitracin synthase 2 Short name=BA2 Including the following 3 domains:
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| Gene names |
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| Organism | Bacillus licheniformis | ||
| Taxonomic identifier | 1402 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 2607 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Activates two amino acids and incorporate a D-ornithine from its second active site into bacitracin. |
| Catalytic activity | L-ornithine = D-ornithine. |
| Cofactor | Binds 2 phosphopantetheines covalently Potential. |
| Pathway | |
| Subunit structure | Large multienzyme complex of BA1, BA2 and BA3. |
| Domain | Consists of two modules with 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 | Bacitracin is a mixture of at least ten cyclic dodecapeptides, that differ by one or two amino acids. The most abundant is bacitracin A, a branched cyclic dodecapeptide. It contains an N-terminal linear pentapeptide moiety (Ile-Cys-Leu-D-Glu-Ile) with an isoleucine-cysteine thiazoline condensation product and a C-terminal heptapeptide ring (Lys-D-Orn-Ile-D-Phe-His-D-Asp-Asn), in which the free alpha-carboxy group of the C-terminal Asn is bound to the epsilon-amino group of Lys. |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. Contains 2 acyl carrier domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic biosynthesis |
| Domain | Repeat |
| Ligand | 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 | acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor bindingInferred from electronic annotation. Source: InterPro ligase activityInferred from electronic annotation. Source: UniProtKB-KW ornithine racemase 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 – 2607 | 2607 | Bacitracin synthase 2 | PRO_0000193083 | |||||
Regions | |||||||||
| Domain | 1021 – 1088 | 68 | Acyl carrier 1 | ||||||
| Domain | 2064 – 2130 | 67 | Acyl carrier 2 | ||||||
| Region | 535 – 1090 | 556 | Domain 1 (lysine-activating) | ||||||
| Region | 1547 – 2141 | 595 | Domain 2 (D-ornithine-activating) | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1051 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 2094 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
Sequences
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References
| [1] | "The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716: molecular characterization of three multi-modular peptide synthetases." Konz D., Klens A., Schoergendorfer K., Marahiel M.A. Chem. Biol. 4:927-937(1997) [PubMed: 9427658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10716 / DSM 603 / NBRC 12199 / NCIMB 8874. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF007865 Genomic DNA. Translation: AAC06347.1. |
| PIR | T31678. |
3D structure databases | |
| ProteinModelPortal | O68007. |
| 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. 2 hits. |
| Pfam | PF00501. AMP-binding. 2 hits. PF00668. Condensation. 3 hits. PF00550. PP-binding. 2 hits. [Graphical view] |
| SUPFAM | SSF47336. ACP_like. 2 hits. |
| TIGRFAMs | TIGR01733. AA-adenyl-dom. 2 hits. TIGR01720. NRPS-para261. 1 hit. |
| PROSITE | PS50075. ACP_DOMAIN. 2 hits. PS00455. AMP_BINDING. 2 hits. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BACB_BACLI | ||||||||
| Accession | Primary (citable) accession number: O68007 | ||||||||
| Entry history |
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| 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 |