Bacteriocin: Microcin C7
Accession: BAC207
Classification
Class: Unclassified
Genetics
Gene: mccA
Producer and target organisms
Producer Organism: Escherichia coli [Gram-negative]
Taxonomy: Bacteria
ProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organismsKlebsiella - Salmonella - Shigella - Yersinia - Proteus - Escherichia coli
Description
Mode of action:
Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp.
Post-translational modification:
The peptide moiety allows entry into the bacterial cell, where it undergoes proteolytic cleavage to release the aspartyl adenylate analog, which is responsible for aspartyl-tRNA synthetase inhibition. Can be processed by the non-specific
oligopeptidases pepA, pepB and pepN.
Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp.
Post-translational modification:
The peptide moiety allows entry into the bacterial cell, where it undergoes proteolytic cleavage to release the aspartyl adenylate analog, which is responsible for aspartyl-tRNA synthetase inhibition. Can be processed by the non-specific
oligopeptidases pepA, pepB and pepN.
Uniprot and PDB links
UniProt Entry: Q47505
PDB Entry3H5R resolved by X-ray 3H9J resolved by X-ray 3H9Q resolved by X-ray
PROTEIN SEQUENCE, AND FUNCTION.
PubMed=2861788;
Garcia-Bustos J.F., Pezzi N., Mendez E.
"Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli.", Antimicrob. Agents Chemother. 27:791-797(1985).
PubMed=2861788;
Garcia-Bustos J.F., Pezzi N., Mendez E.
"Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli.", Antimicrob. Agents Chemother. 27:791-797(1985).
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
MEDLINE=94239518;PubMed=8183363;DOI=10.1038/369281a0
Gonzalez-Pastor J.E., San Millan J.L., Moreno F.
"The smallest known gene.", Nature 369:281-281(1994).
MEDLINE=94239518;PubMed=8183363;DOI=10.1038/369281a0
Gonzalez-Pastor J.E., San Millan J.L., Moreno F.
"The smallest known gene.", Nature 369:281-281(1994).
PROTEIN SEQUENCE, MASS SPECTROMETRY, FORMYLATION AT MET-1, AND ASPARTIC ACID 1-[(3-AMINOPROPYL)(5'-ADENOSYL)PHOSPHONO]AMIDE FORMATION AT ASN-7.
PubMed=7835418;DOI=10.1016/0014-5793(94)01345-2
Metlitskaya A.Z., Katrukha G.S., Shashkov A.S., Zaitsev D.A., Egorov T.A., Khmel I.A.
"Structure of microcin C51, a new antibiotic with a broad spectrum of activity.", FEBS Lett. 357:235-238(1995).
PubMed=7835418;DOI=10.1016/0014-5793(94)01345-2
Metlitskaya A.Z., Katrukha G.S., Shashkov A.S., Zaitsev D.A., Egorov T.A., Khmel I.A.
"Structure of microcin C51, a new antibiotic with a broad spectrum of activity.", FEBS Lett. 357:235-238(1995).
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
MEDLINE=96099297;PubMed=8522520;
Gonzalez-Pastor J.E., San Millan J.L., Castilla M.A., Moreno F.
"Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7.", J. Bacteriol. 177:7131-7140(1995).
MEDLINE=96099297;PubMed=8522520;
Gonzalez-Pastor J.E., San Millan J.L., Castilla M.A., Moreno F.
"Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7.", J. Bacteriol. 177:7131-7140(1995).
FUNCTION.
PubMed=16574659;DOI=10.1074/jbc.M513174200
Metlitskaya A.Z., Kazakov T., Kommer A., Pavlova O., Praetorius-Ibba M., Ibba M., Krasheninnikov I., Kolb V., Khmel I.A., Severinov K.
"Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic microcin C.", J. Biol. Chem. 281:18033-18042(2006).
PubMed=16574659;DOI=10.1074/jbc.M513174200
Metlitskaya A.Z., Kazakov T., Kommer A., Pavlova O., Praetorius-Ibba M., Ibba M., Krasheninnikov I., Kolb V., Khmel I.A., Severinov K.
"Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic microcin C.", J. Biol. Chem. 281:18033-18042(2006).
REVIEW.
PubMed=17827970;DOI=10.1159/000104748
Duquesne S., Petit V., Peduzzi J., Rebuffat S.
"Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria.", J. Mol. Microbiol. Biotechnol. 13:200-209(2007).
PubMed=17827970;DOI=10.1159/000104748
Duquesne S., Petit V., Peduzzi J., Rebuffat S.
"Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria.", J. Mol. Microbiol. Biotechnol. 13:200-209(2007).
REVIEW.
PubMed=17711420;DOI=10.1111/j.1365-2958.2007.05874.x
Severinov K., Semenova E., Kazakov A., Kazakov T., Gelfand M.S.
"Low-molecular-weight post-translationally modified microcins.", Mol. Microbiol. 65:1380-1394(2007).
PubMed=17711420;DOI=10.1111/j.1365-2958.2007.05874.x
Severinov K., Semenova E., Kazakov A., Kazakov T., Gelfand M.S.
"Low-molecular-weight post-translationally modified microcins.", Mol. Microbiol. 65:1380-1394(2007).
FUNCTION, AND PROTEOLYTIC PROCESSING.
PubMed=18223070;DOI=10.1128/JB.01956-07
Kazakov T., Vondenhoff G.H., Datsenko K.A., Novikova M., Metlitskaya A.Z., Wanner B.L., Severinov K.
"Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C.", J. Bacteriol. 190:2607-2610(2008).
PubMed=18223070;DOI=10.1128/JB.01956-07
Kazakov T., Vondenhoff G.H., Datsenko K.A., Novikova M., Metlitskaya A.Z., Wanner B.L., Severinov K.
"Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C.", J. Bacteriol. 190:2607-2610(2008).
STRUCTURE BY NMR, FUNCTION, MASS SPECTROMETRY, FORMYLATION AT MET-1, AND ASPARTIC ACID 1-[(3-AMINOPROPYL)(5'-ADENOSYL)PHOSPHONO]AMIDE FORMATION AT ASN-7.
PubMed=7559516;DOI=10.1074/jbc.270.40.23520
Guijarro J.I., Gonzalez-Pastor J.E., Baleux F., San Millan J.L., Castilla M.A., Rico M., Moreno F., Delepierre M.
"Chemical structure and translation inhibition studies of the antibiotic microcin C7.", J. Biol. Chem. 270:23520-23532(1995).
PubMed=7559516;DOI=10.1074/jbc.270.40.23520
Guijarro J.I., Gonzalez-Pastor J.E., Baleux F., San Millan J.L., Castilla M.A., Rico M., Moreno F., Delepierre M.
"Chemical structure and translation inhibition studies of the antibiotic microcin C7.", J. Biol. Chem. 270:23520-23532(1995).
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Gene structure
| Gene id | Name | Description | Location |
| BACGene935 | mccA | structure of microcin C7 | 203..226 |
| BACGene936 | mccB | production of microcin C7 | 301..1353 |
| BACGene937 | mccC | production of microcin C7 valine start | 1350..2564 |
| BACGene938 | mccD | production of microcin C7 | 2561..3364 |
| BACGene939 | mccD | ORF87 | 3349..3612 |
| BACGene940 | mccE | production and immunity | 3552..5117 |
| BACGene941 | mccF | immunity | complement(5173..6207) |
Protein sequence
| ........10 | MRTGNAN |
Wheel representation
3D Structure
View PDB entry: 3H5R
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔7 | 7 | Microcin C7. Feature identifier = PRO_0000341532. |
| Modified residue | 1 | N-formylmethionine. | |
| Modified residue | 7 | Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide. | |
| STRAND | 3↔5 | 3 |
Composition
| Amino acid | Count | Percent |
|---|---|---|
| A | 1 | 14.29 % |
| C | 0 | 0.00 % |
| D | 0 | 0.00 % |
| E | 0 | 0.00 % |
| F | 0 | 0.00 % |
| G | 1 | 14.29 % |
| H | 0 | 0.00 % |
| I | 0 | 0.00 % |
| K | 0 | 0.00 % |
| L | 0 | 0.00 % |
| M | 1 | 14.29 % |
| N | 2 | 28.57 % |
| P | 0 | 0.00 % |
| Q | 0 | 0.00 % |
| R | 1 | 14.29 % |
| S | 0 | 0.00 % |
| T | 1 | 14.29 % |
| V | 0 | 0.00 % |
| W | 0 | 0.00 % |
| Y | 0 | 0.00 % |
Hydrophobicity
Composition
| Formula | C0
H0
N0
O0
S0 |
| Absent amino acids | CDEFHIKLPQSVWY |
| Common amino acids | N |
| Mass (Da) | 1177 |
| Net charge | +1 |
| Isoelectric point | 10.55 |
| Basic residues | 1 |
| Acidic residues | 0 |
| Hydrophobic residues | 1 |
| Polar residues | 4 |
| Aliphatic residues | 0 |
| Tiny residues | 2 |
| Boman Index | -25.67 |
| Hydropathy Index | -1.271 |
| Aliphatic Index | 14.29 |
| Instability Index | -26.46 (stable) |
| Half Life |
Mammalian : 30 hour Yeast : >20 hour E. coli : >10 hour |
| Extinction Coefficient | 0 M-1 cm-1 |
| Absorbance 280nm | 0 |