Bacteriocin: Microcin C7

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Bacteriocin: Microcin C7

Accession: BAC207

Classification
Class: Unclassified
Genetics
Gene: mccA
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.
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).
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).
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).
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).
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).
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).
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).
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End Note
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BibTeX
Gene structure
genome of Microcin C7

Gene idNameDescriptionLocation
BACGene935mccAstructure of microcin C7203..226
BACGene936mccBproduction of microcin C7301..1353
BACGene937mccCproduction of microcin C7 valine start1350..2564
BACGene938mccDproduction of microcin C72561..3364
BACGene939mccDORF873349..3612
BACGene940mccEproduction and immunity3552..5117
BACGene941mccFimmunitycomplement(5173..6207)
mccAmccBmccCmccDmccDmccEmccF
Protein sequence
 ........10 
          | 
 MRTGNAN

Wheel representation
wheel representation of Microcin C7
3D Structure
Protein sequence annotations
Features of Microcin C7

MN
FeaturePosition(s)LengthDescription
PEPTIDE1↔77
Microcin C7.
Feature identifier = PRO_0000341532.
Modified residue1N-formylmethionine.
Modified residue7Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide.
STRAND3↔53
Composition
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

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