Reviewed,
UniProtKB/Swiss-Prot Q9X2V7 (MCJA_ECOLX)
Last modified
January 19, 2010.
Version 45.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (2) |
 Third-party data |
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Names and origin
| Protein names | Recommended name: Microcin J25 Short name=MccJ25 | ||
| Gene names |
| ||
| Encoded on | Plasmid pTUC100 | ||
| Organism | Escherichia coli | ||
| Taxonomic identifier | 562 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 58 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). May inhibit transcription by binding in RNAP secondary channel and blocking nucleotide substrates access to the catalytic center. Exhibits potent bacteriocidal activity against a range of Enterobacteriaceae, including several pathogenic E.coli, Salmonella and Shigella strains. Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. Induces bacterial filamentation in susceptible cells in a non-SOS-dependent way, but this phenotype may result from impaired transcription of genes coding for cell division proteins. Ref.4 Ref.5 Ref.6 |
| Subcellular location | |
| Induction | At the onset of stationary growth phase. |
| Caution | Was originally (Ref.2) thought to have a head-to-tail cyclic structure, but actually has a threaded side chain-to-backbone ring structure that is penetrated by the C-terminal tail in a noose-like motif. |
| Mass spectrometry | Molecular mass is 2107.0 Da from positions 38 - 58. Determined by ESI. Ref.2 Molecular mass is 2106.0 Da from positions 38 - 58. Determined by MALDI. Ref.8 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Antibiotic Antimicrobial Bacteriocin |
| PTM | Isopeptide bond |
| Technical term | 3D-structure Direct protein sequencing Plasmid |
| Gene Ontology (GO) | |
| Biological process | cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | receptor binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 37 | 37 | PRO_0000002774 | ||||||||
| Peptide | 38 – 58 | 21 | Microcin J25 Ref.2 | PRO_0000002775 | |||||||
Amino acid modifications | |||||||||||
| Cross-link | 38 ↔ 45 | Isoglutamyl glycine isopeptide (Gly-Glu) | |||||||||
Secondary structure | |||||||||||
Helix Strand Turn | |||||||||||
| Beta strand | 41 – 44 | 4 | |||||||||
Sequences
References
| [1] | "Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25." Solbiati J.O., Ciaccio M., Farias R.N., Gonzalez-Pastor J.E., Moreno F., Salomon R.A. J. Bacteriol. 181:2659-2662(1999) [PubMed: 10198038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AY25. |
| [2] | "The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli." Blond A., Peduzzi J., Goulard C., Chiuchiolo M.J., Barthelemy M., Prigent Y., Salomon R.A., Farias R.N., Moreno F., Rebuffat S. Eur. J. Biochem. 259:747-755(1999) [PubMed: 10092860] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-58, MASS SPECTROMETRY. |
| [3] | "Microcin 25, a novel antimicrobial peptide produced by Escherichia coli." Salomon R.A., Farias R.N. J. Bacteriol. 174:7428-7435(1992) [PubMed: 1429464] [Abstract] Cited for: CHARACTERIZATION. |
| [4] | "The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport." Rintoul M.R., de Arcuri B.F., Salomon R.A., Farias R.N., Morero R.D. FEMS Microbiol. Lett. 204:265-270(2001) [PubMed: 11731133] [Abstract] Cited for: FUNCTION. |
| [5] | "Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25." Delgado M.A., Rintoul M.R., Farias R.N., Salomon R.A. J. Bacteriol. 183:4543-4550(2001) [PubMed: 11443089] [Abstract] Cited for: FUNCTION. |
| [6] | "Mutations of bacterial RNA polymerase leading to resistance to microcin J25." Yuzenkova J., Delgado M.A., Nechaev S., Savalia D., Epshtein V., Artsimovitch I., Mooney R.A., Landick R., Farias R.N., Salomon R.A., Severinov K. J. Biol. Chem. 277:50867-50875(2002) [PubMed: 12401787] [Abstract] Cited for: FUNCTION. |
| [7] | "Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot." Bayro M.J., Mukhopadhyay J., Swapna G.V.T., Huang J.Y., Ma L.-C., Sineva E., Dawson P.E., Montelione G.T., Ebright R.H. J. Am. Chem. Soc. 125:12382-12383(2003) [PubMed: 14531661] [Abstract] Cited for: MASS SPECTROMETRY, STRUCTURE BY NMR OF 38-58. |
| [8] | "Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone." Rosengren K.J., Clark R.J., Daly N.L., Goeransson U., Jones A., Craik D.J. J. Am. Chem. Soc. 125:12464-12474(2003) [PubMed: 14531690] [Abstract] Cited for: CHARACTERIZATION, MASS SPECTROMETRY, STRUCTURE BY NMR OF 38-58. |
| [9] | "Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail." Wilson K.-A., Kalkum M., Ottesen J., Yuzenkova J., Chait B.T., Landick R., Muir T., Severinov K., Darst S.A. J. Am. Chem. Soc. 125:12475-12483(2003) [PubMed: 14531691] [Abstract] Cited for: MASS SPECTROMETRY, STRUCTURE BY NMR OF 38-58. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF061787 Genomic DNA. Translation: AAD28494.1. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||||||||
| TCDB | 9.A.52.1.1. microcin J25 (Microsin J25) family. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | MCJA_ECOLX | ||||||||
| Accession | Primary (citable) accession number: Q9X2V7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |
