Q9X2V7 (MCJA_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Microcin J25
Short name=MccJ25

Gene names

Name:

mcjA

Encoded on

Plasmid pTUC100

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	58 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). May inhibit transcription by binding in RNAP secondary channel and blocking nucleotide substrates access to the catalytic center. Exhibits potent bacteriocidal activity against a range of Enterobacteriaceae, including several pathogenic E.coli, Salmonella and Shigella strains. Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. Induces bacterial filamentation in susceptible cells in a non-SOS-dependent way, but this phenotype may result from impaired transcription of genes coding for cell division proteins. Ref.4 Ref.5 Ref.6
Subcellular location	Secreted.
Induction	At the onset of stationary growth phase.
Caution	Was originally (Ref.2) thought to have a head-to-tail cyclic structure, but actually has a threaded side chain-to-backbone ring structure that is penetrated by the C-terminal tail in a noose-like motif.
Mass spectrometry	Molecular mass is 2107.0 Da from positions 38 - 58. Determined by ESI. Ref.2 Molecular mass is 2106.0 Da from positions 38 - 58. Determined by MALDI. Ref.8

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Antibiotic Antimicrobial Bacteriocin
PTM	Isopeptide bond
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological_process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 37

37

PRO_0000002774

Peptide

38 – 58

21

Microcin J25 Ref.2

PRO_0000002775

Amino acid modifications

Cross-link

38 ↔ 45

Isoglutamyl glycine isopeptide (Gly-Glu)

Secondary structure

1

.

.

.

.

.

.

.

58

Helix Strand Turn

Details...

Beta strand

42 – 44

3

Beta strand

48 – 51

4

Beta strand

55 – 57

3

Sequences

	Sequence		Length	Mass (Da)
	Q9X2V7 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: A9F4393C8EAAC8FA	FASTA	58	6,200
	10 20 30 40 50 MIKHFHFNKL SSGKKNNVPS PAKGVIQIKK SASQLTKGGA GHVPEYFVGI GTPISFYG

References

[1]	"Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25." Solbiati J.O., Ciaccio M., Farias R.N., Gonzalez-Pastor J.E., Moreno F., Salomon R.A. J. Bacteriol. 181:2659-2662(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AY25.
[2]	"The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli." Blond A., Peduzzi J., Goulard C., Chiuchiolo M.J., Barthelemy M., Prigent Y., Salomon R.A., Farias R.N., Moreno F., Rebuffat S. Eur. J. Biochem. 259:747-755(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-58, MASS SPECTROMETRY.
[3]	"Microcin 25, a novel antimicrobial peptide produced by Escherichia coli." Salomon R.A., Farias R.N. J. Bacteriol. 174:7428-7435(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[4]	"The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport." Rintoul M.R., de Arcuri B.F., Salomon R.A., Farias R.N., Morero R.D. FEMS Microbiol. Lett. 204:265-270(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25." Delgado M.A., Rintoul M.R., Farias R.N., Salomon R.A. J. Bacteriol. 183:4543-4550(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Mutations of bacterial RNA polymerase leading to resistance to microcin J25." Yuzenkova J., Delgado M.A., Nechaev S., Savalia D., Epshtein V., Artsimovitch I., Mooney R.A., Landick R., Farias R.N., Salomon R.A., Severinov K. J. Biol. Chem. 277:50867-50875(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot." Bayro M.J., Mukhopadhyay J., Swapna G.V.T., Huang J.Y., Ma L.-C., Sineva E., Dawson P.E., Montelione G.T., Ebright R.H. J. Am. Chem. Soc. 125:12382-12383(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, STRUCTURE BY NMR OF 38-58.
[8]	"Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone." Rosengren K.J., Clark R.J., Daly N.L., Goeransson U., Jones A., Craik D.J. J. Am. Chem. Soc. 125:12464-12474(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, MASS SPECTROMETRY, STRUCTURE BY NMR OF 38-58.
[9]	"Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail." Wilson K.-A., Kalkum M., Ottesen J., Yuzenkova J., Chait B.T., Landick R., Muir T., Severinov K., Darst S.A. J. Am. Chem. Soc. 125:12475-12483(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, STRUCTURE BY NMR OF 38-58.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Entanglement - Issue 72 of July 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF061787 Genomic DNA. Translation: AAD28494.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PP5	NMR	-	A	38-58	[»]
1Q71	NMR	-	A	38-58	[»]
1S7P	NMR	-	A	38-47	[»]
			B	48-58	[»]

ModBase

Search...

Protein family/group databases

TCDB

9.A.52.1.1. microcin J25 (Microsin J25) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X2V7.

Entry information

Entry name

MCJA_ECOLX

Accession

Primary (citable) accession number: Q9X2V7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	November 1, 1999
Last modified:	April 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program