AMPDB_412 | Microcin J25

1 General Description

AMPDB ID: AMPDB_412

Protein Names: Microcin J25 (MccJ25) (Class II lasso peptide) (Ribosomally synthesized and post-translationally modified peptide) (RiPP)

Protein Family: Nil

Gene Name: mcjA

Source Organism: Escherichia coli

Protein Length: 58 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MIKHFHFNKLSSGKKNNVPSPAKGVIQIKKSASQLTKGGAGHVPEYFVGIGTPISFYG

FASTA format

Counts of Amino Acids

'A': 3, 'R': 0, 'N': 3, 'D': 0, 'C': 0, 'Q': 2, 'E': 1, 'G': 8, 'H': 3, 'I': 5, 'L': 2, 'K': 8, 'M': 1, 'F': 4, 'P': 4, 'S': 6, 'T': 2, 'W': 0, 'Y': 2, 'V': 4

Frequencies of Amino Acids

'A': 5.17%, 'R': 0%, 'N': 5.17%, 'D': 0%, 'C': 0%, 'Q': 3.45%, 'E': 1.72%, 'G': 13.79%, 'H': 5.17%, 'I': 8.62%, 'L': 3.45%, 'K': 13.79%, 'M': 1.72%, 'F': 6.9%, 'P': 6.9%, 'S': 10.34%, 'T': 3.45%, 'W': 0%, 'Y': 3.45%, 'V': 6.9%

Missing Amino Acid(s)

C, D, R, W

Most Occurring Amino Acid(s)

G, K

Less Occurring Amino Acid(s)

E, M

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	6200.21 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	72.241	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	32.478	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.255	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.606	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	10.865	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	7.268	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.293, 0.362, 0.121 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.103	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	2980, 2980	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

E.coli (Gram-negative), Enterobacteriaceae (Gram-negative), Salmonella (Gram-negative), Shigella (Gram-negative)

4.2 Antimicrobial Activity

Antibiotic, Antimicrobial, Bacteriocin, 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: Solbiati JO, Ciaccio M, FarÃas RN, et al. Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25. J Bacteriol. 1999;181(8):2659-62. Published 1999 Apr. doi:10.1128/JB.181.8.2659-2662.1999

PMID: 10198038

Citation 2: Blond A, PÃ©duzzi J, Goulard C, et al. The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli. Eur J Biochem. 1999;259(3):747-55. Published 1999 Feb. doi:10.1046/j.1432-1327.1999.00085.x

PMID: 10092860

Citation 3: SalomÃ³n RA, FarÃas RN, FarÃas RN. Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. J Bacteriol. 1992;174(22):7428-35. Published 1992 Nov. doi:10.1128/jb.174.22.7428-7435.1992

PMID: 1429464

Citation 4: Rintoul MR, de Arcuri BF, SalomÃ³n RA, et al. The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport. FEMS Microbiol Lett. 2001;204(2):265-70. Published 2001 Nov 13. doi:10.1111/j.1574-6968.2001.tb10895.x

PMID: 11731133

Citation 5: Delgado MA, Rintoul MR, FarÃas RN, et al. Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25. J Bacteriol. 2001;183(15):4543-50. Published 2001 Aug. doi:10.1128/JB.183.15.4543-4550.2001

PMID: 11443089

Citation 6: Yuzenkova J, Delgado M, Nechaev S, et al. Mutations of bacterial RNA polymerase leading to resistance to microcin j25. J Biol Chem. 2002;277(52):50867-75. Published 2002 Dec 27. doi:10.1074/jbc.M209425200

PMID: 12401787

Citation 7: Mukhopadhyay J, Sineva E, Knight J, et al. Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel. Mol Cell. 2004;14(6):739-51. Published 2004 Jun 18. doi:10.1016/j.molcel.2004.06.010

PMID: 15200952

Citation 8: Pavlova O, Mukhopadhyay J, Sineva E, et al. Systematic structure-activity analysis of microcin J25. J Biol Chem. 2008;283(37):25589-25595. Published 2008 Sep 12. doi:10.1074/jbc.M803995200

PMID: 18632663

Citation 9: Bayro MJ, Mukhopadhyay J, Swapna GV, et al. Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot. J Am Chem Soc. 2003;125(41):12382-3. Published 2003 Oct 15. doi:10.1021/ja036677e

PMID: 14531661

Citation 10: Rosengren KJ, Clark RJ, Daly NL, et al. Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone. J Am Chem Soc. 2003;125(41):12464-74. Published 2003 Oct 15. doi:10.1021/ja0367703

PMID: 14531690

Citation 11: Wilson KA, Kalkum M, Ottesen J, et al. Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail. J Am Chem Soc. 2003;125(41):12475-83. Published 2003 Oct 15. doi:10.1021/ja036756q

PMID: 14531691

Citation 12: Braffman NR, Piscotta FJ, Hauver J, et al. Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin. Proc Natl Acad Sci U S A. 2019;116(4):1273-1278. Published 2019 Jan 22. doi:10.1073/pnas.1817352116

PMID: 30626643

5.2 Protein Sequence Databases

5.3 3D Structure Databases

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

AlphaFoldDB: Q9X2V7

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	AF061787	GenBank \|\| EMBL

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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