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Protein

Microcin C7

Gene

mccA

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Antibacterial peptide, active against enterobacteria including species of Klebsiella, Salmonella, Shigella, Yersinia and Proteus, and strains of E.coli. Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp.5 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Names & Taxonomyi

Protein namesi
Recommended name:
Microcin C7
Short name:
MccC7
Alternative name(s):
Microcin C51
Short name:
McC
Short name:
MccC51
Short name:
Microcin C
Gene namesi
Name:mccAImported
Encoded oniPlasmid pMccC7Imported
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 77Microcin C72 PublicationsPRO_0000341532

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionine2 Publications
Modified residuei7 – 71Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide2 Publications

Post-translational modificationi

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.4 Publications

Keywords - PTMi

Formylation, Phosphoprotein

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
mccBQ475068EBI-7035319,EBI-7035293

Protein-protein interaction databases

IntActiQ47505. 1 interaction.
MINTiMINT-7265788.

Structurei

Secondary structure

1
7
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H5RX-ray2.10E/F/G/H1-7[»]
3H9GX-ray2.20E/F/G/H1-7[»]
3H9JX-ray2.30E/F/G/H1-7[»]
3H9QX-ray2.63E/F/G/H1-7[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ47505.

Sequencei

Sequence statusi: Complete.

Length:7
Mass (Da):763
Last modified:November 1, 1996 - v1
Checksum:i644DD44861B406F0
GO

Mass spectrometryi

Molecular mass is 1177±1 Da from positions 1 - 7. Determined by ESI. 2 Publications
Molecular mass is 1177.5 Da from positions 1 - 7. Determined by PD. 2 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57583 Genomic DNA. Translation: CAA40808.1.
PIRiS45311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57583 Genomic DNA. Translation: CAA40808.1.
PIRiS45311.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H5RX-ray2.10E/F/G/H1-7[»]
3H9GX-ray2.20E/F/G/H1-7[»]
3H9JX-ray2.30E/F/G/H1-7[»]
3H9QX-ray2.63E/F/G/H1-7[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ47505. 1 interaction.
MINTiMINT-7265788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ47505.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli."
    Garcia-Bustos J.F., Pezzi N., Mendez E.
    Antimicrob. Agents Chemother. 27:791-797(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure of microcin C51, a new antibiotic with a broad spectrum of activity."
    Metlitskaya A.Z., Katrukha G.S., Shashkov A.S., Zaitsev D.A., Egorov T.A., Khmel I.A.
    FEBS Lett. 357:235-238(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, FORMYLATION AT MET-1, PHOSPHORAMIDE AT ASN-7.
  4. "Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7."
    Gonzalez-Pastor J.E., San Millan J.L., Castilla M.A., Moreno F.
    J. Bacteriol. 177:7131-7140(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Cited for: FUNCTION.
  6. "Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria."
    Duquesne S., Petit V., Peduzzi J., Rebuffat S.
    J. Mol. Microbiol. Biotechnol. 13:200-209(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  7. "Low-molecular-weight post-translationally modified microcins."
    Severinov K., Semenova E., Kazakov A., Kazakov T., Gelfand M.S.
    Mol. Microbiol. 65:1380-1394(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C."
    Kazakov T., Vondenhoff G.H., Datsenko K.A., Novikova M., Metlitskaya A.Z., Wanner B.L., Severinov K.
    J. Bacteriol. 190:2607-2610(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC PROCESSING.
  9. "Chemical structure and translation inhibition studies of the antibiotic microcin C7."
    Guijarro J.I., Gonzalez-Pastor J.E., Baleux F., San Millan J.L., Castilla M.A., Rico M., Moreno F., Delepierre M.
    J. Biol. Chem. 270:23520-23532(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, FUNCTION, MASS SPECTROMETRY, FORMYLATION AT MET-1, PHOSPHORAMIDE AT ASN-7.

Entry informationi

Entry nameiMCCC7_ECOLX
AccessioniPrimary (citable) accession number: Q47505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.