Microcin E492

Accession: BAC119

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Bacteriocin: Microcin E492

Accession: BAC119

Classification

Class: ~~Unclassified~~

Genetics

Gene: mceA

Producer and target organisms

Producer Organism: Klebsiella pneumoniae [Gram-negative]

Taxonomy: BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Target organismsenterobacteria

Description

Mode of action:
Channel-forming bacteriocin. Forms cation-selective channels.

Post-translational modification:
The C-terminal Ser is modified by attachment to a siderophore similar to enterobactin, which can bind one atom of iron. The modification consists of an ester linkage of the serine carboxyl to O6 of a glucose which is linked by a C-glycosidic bond to the 5'-benzoyl of a linear triester of N-(2,3-dihydroxybenzoyl)serine. RANGE=20-103; NOTE=Ref.2. 103 unmodified form (Ref.3). 103 modified form (Ref.3).

Uniprot and PDB links

UniProt Entry: Q9Z4N4 P82962

PDB Entry~~Unknown~~

[Ref. 1] | View abstract | Export citation

NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION, STRAIN=RYC492
MEDLINE=99084959;PubMed=9864332;
Lagos R., Villanueva J.E., Monasterio O.
"Identification and properties of the genes encoding microcin E492 and its immunity protein.", J. Bacteriol. 181:212-217(1999).

[Ref. 2]

PROTEIN SEQUENCE OF 20-103, AND MASS SPECTROMETRY.
Pons A.M., Vignon D., Cottenceau G.
"", Submitted (FEB-2001) to Swiss-Prot.

[Ref. 3] | View abstract | Export citation

PARTIAL PROTEIN SEQUENCE, AMINO-ACID COMPOSITION, SIDEROPHORE BINDING SITE, AND MASS SPECTROMETRY, STRAIN=RYC492
PubMed=15102848;DOI=10.1074/jbc.M400228200
Thomas X., Destoumieux-Garzon D., Peduzzi J., Afonso C., Blond A., Birlirakis N., Goulard C., Dubost L., Thai R., Tabet J.-C., Rebuffat S.
"Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity.", J. Biol. Chem. 279:28233-28242(2004).

[Ref. 4] | View abstract | Export citation

CHARACTERIZATION, STRAIN=RYC492
MEDLINE=93238942;PubMed=7682973;DOI=10.1016/0014-5793(93)80096-D
Lagos R., Wilkens M., Vergara C., Cecchi X., Monasterio O.
"Microcin E492 forms ion channels in phospholipid bilayer membrane.", FEBS Lett. 321:145-148(1993).

Gene structure

Gene id	Name	Description	Location
BACGene554	mceA	microcin E492 precursor channel-forming bacteriocin MceA; overlapping with mceB	complement(255..554)
BACGene555	mceB	microcin E492 immunity protein MceB; overlapping with mceA	complement(541..828)
BACGene556	mceC	MceC required for microcin E492 modification enterochelin glycosyl transferase; similar to IroB	1306..2418
BACGene557	mceD	MceD apo and ferric salmochelin esterase similar to IroD	complement(2597..3841)
BACGene558	mceD	MceS2 similar to MchS2, microcin I47 precursor	complement(3918..4085)
BACGene559	mceD	MceS3 similar to MchS3, microcin I47 immunity protein	complement(4315..4521)
BACGene560	mceD	MceM	complement(4683..4940)
BACGene561	mceD	MceL putative bacteriocin N- and C-termini similar to the microcin E492, I47, H47 and M precursors MceA,MchS2, MchB and McmA	complement(4962..5231)
BACGene562	mceE	MceE C-terminus similar to MchS4, which promotes enterochelin production	complement(5371..5715)
BACGene563	mceE	MceX similar to MshX	5936..6043
BACGene564	mceJ	MceJ required for microcin E492 modification with salmochelin	6182..7756
BACGene565	mceI	MceI required for microcin E492 modification with salmochelin similar to toxin-activating protein C, leukotoxin C	7769..8260
BACGene566	mceH	MceH second component of microcin E492 exporter membrane-fusion protein; similar to CvaA, the second component of colicin Vexporter	8419..9660
BACGene567	mceG	MceG ABC protein of microcin E492 exporter microcin leader peptide processing similar to CvaB, an ABC exporter of colicin V	9653..11749
BACGene568	mceG	MceK putative fusion protein; N-terminus similar to McmI, microcin M immunityprotein; C-terminus similar to McmA, microcin M precursor	11793..12203
BACGene569	mceF	MceF similar to McmM of CAAX amino terminal protease family	complement(12400..13092)

Protein sequence

........10 ........20 ........30 ........40 ........50 ........60 ........70 ........80
| | | | | | | |
GETDPNTQLL NDLGNNMAWG AALGAPGGLG SAALGAAGGA LQTVGQGLID HGPVNVPIPV LIGPSWNGSG SGYNSATSSS
GSGS

Wheel representation

Protein sequence annotations

Feature	Position(s)	Length	Description
CHAIN	1↔84	84	Microcin E492. Feature identifier = PRO_0000005677.
Modified residue	84		Serine microcin E492 siderophore ester.

Composition

Amino acid	Count	Percent
A	10	11.90 %
C	0	0.00 %
D	3	3.57 %
E	1	1.19 %
F	0	0.00 %
G	19	22.62 %
H	1	1.19 %
I	3	3.57 %
K	0	0.00 %
L	9	10.71 %
M	1	1.19 %
N	7	8.33 %
P	6	7.14 %
Q	3	3.57 %
R	0	0.00 %
S	10	11.90 %
T	4	4.76 %
V	4	4.76 %
W	2	2.38 %
Y	1	1.19 %

Hydrophobicity

Composition

Formula	C₃₃₈ H₅₃₀ N₉₈ O₁₁₈ S₁
Absent amino acids	CFKR
Common amino acids	G
Mass (Da)	7906.02
Net charge	-3
Isoelectric point	3.7
Basic residues	1
Acidic residues	4
Hydrophobic residues	28
Polar residues	41
Aliphatic residues	16
Tiny residues	39
Boman Index	-26.98
Hydropathy Index	0.01
Aliphatic Index	81.43
Instability Index	21.21 (stable)
Half Life	Mammalian : 30 hour Yeast : >20 hour E. coli : >10 hour
Extinction Coefficient	12490 M^-1 cm^-1
Absorbance 280nm	150.48