AMPDB_4402 | Microcin C7

1 General Description

AMPDB ID: AMPDB_4402

Protein Names: Microcin C7 (MccC7) (Microcin C51) (McC) (MccC51) (Microcin C)

Protein Family: Nil

Gene Name: mccA

Source Organism: Escherichia coli

Protein Length: 7 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MRTGNAN

FASTA format

Counts of Amino Acids

'A': 1, 'R': 1, 'N': 2, 'D': 0, 'C': 0, 'Q': 0, 'E': 0, 'G': 1, 'H': 0, 'I': 0, 'L': 0, 'K': 0, 'M': 1, 'F': 0, 'P': 0, 'S': 0, 'T': 1, 'W': 0, 'Y': 0, 'V': 0

Frequencies of Amino Acids

'A': 14.29%, 'R': 14.29%, 'N': 28.57%, 'D': 0%, 'C': 0%, 'Q': 0%, 'E': 0%, 'G': 14.29%, 'H': 0%, 'I': 0%, 'L': 0%, 'K': 0%, 'M': 14.29%, 'F': 0%, 'P': 0%, 'S': 0%, 'T': 14.29%, 'W': 0%, 'Y': 0%, 'V': 0%

Missing Amino Acid(s)

C, D, E, F, H, I, K, L, P, Q, S, V, W, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

A, G, M, R, T

Hydrophobic Amino Acid(s) Count

Hydrophilic Amino Acid(s) Count

Basic Amino Acid(s) Count

Acidic Amino Acid(s) Count

Modified Amino Acid(s) Count

Modified Amino Acid(s) Frequencies

Computed by biopython (version 1.79) & proteinAnalysis (version 1)

3 Physicochemical Properties

Sl. No.	Properties	Values	Reference
1.	Molecular Mass	762.839 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	14.286	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	-26.457	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-1.271	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.345	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	10.55	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	0.998	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0, 0.429, 0.286 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	0, 0	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Klebsiella (Gram-negative), Proteus (Gram-negative), Salmonella (Gram-negative), Shigella (Gram-negative), Yersinia (Gram-negative)

4.2 Antimicrobial Activity

Antibiotic, Antimicrobial, Anti-gram-negative

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Non-hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Garcia-Bustos JF, Pezzi N, Mendez E, et al. Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli. Antimicrob Agents Chemother. 1985;27(5):791-7. Published 1985 May. doi:10.1128/AAC.27.5.791

PMID: 2861788

Citation 2: GonzÃ¡lez-Pastor JE, San MillÃ¡n JL, Moreno F, et al. The smallest known gene. Nature. 1994;369(6478):281. Published 1994 May 26. doi:10.1038/369281a0

PMID: 8183363

Citation 3: Metlitskaya AZ, Katrukha GS, Shashkov AS, et al. Structure of microcin C51, a new antibiotic with a broad spectrum of activity. FEBS Lett. 1995;357(3):235-8. Published 1995 Jan 9. doi:10.1016/0014-5793(94)01345-2

PMID: 7835418

Citation 4: GonzÃ¡lez-Pastor JE, San MillÃ¡n JL, Castilla MA, et al. Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7. J Bacteriol. 1995;177(24):7131-40. Published 1995 Dec. doi:10.1128/jb.177.24.7131-7140.1995

PMID: 8522520

Citation 5: Metlitskaya A, Kazakov T, Kommer A, et al. Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic Microcin C. J Biol Chem. 2006;281(26):18033-42. Published 2006 Jun 30. doi:10.1074/jbc.M513174200

PMID: 16574659

Citation 6: Duquesne S, Petit V, Peduzzi J, et al. Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria. J Mol Microbiol Biotechnol. 2007;13(4):200-9. Published 2007. doi:10.1159/000104748

PMID: 17827970

Citation 7: Severinov K, Semenova E, Kazakov A, et al. Low-molecular-weight post-translationally modified microcins. Mol Microbiol. 2007;65(6):1380-94. Published 2007 Sep. doi:10.1111/j.1365-2958.2007.05874.x

PMID: 17711420

Citation 8: Kazakov T, Vondenhoff GH, Datsenko KA, et al. Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C. J Bacteriol. 2008;190(7):2607-10. Published 2008 Apr. doi:10.1128/JB.01956-07

PMID: 18223070

Citation 9: Guijarro JI, GonzÃ¡lez-Pastor JE, Baleux F, et al. Chemical structure and translation inhibition studies of the antibiotic microcin C7. J Biol Chem. 1995;270(40):23520-32. Published 1995 Oct 6. doi:10.1074/jbc.270.40.23520

PMID: 7559516

5.2 Protein Sequence Databases

5.3 3D Structure Databases

	Sl. no.	PDB ID	Method	Resolution	Access Links	3D View

AlphaFoldDB: Q47505

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	X57583	GenBank \|\| EMBL

RefSeq: Not found

5.5 Protein-Protein Interaction Databases

STRING: Not found

BioGRID: Not found

5.6 Ligand Databases

BindingDB: Not found

DrugBank: Not found

ChEMBL: Not found

5.7 Family & Domain Databases

InterPro: Not found

PANTHER: Not found

PROSITE: Not found

5.8 Genome Annotation Databases

Ensembl: Not found

5.9 Phylogenomic Databases

GeneTree: Not found

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: Not found

5.11 Protein-RNA Interaction Databases

RNAct: Not found

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