MCEA_KLEPN
ID MCEA_KLEPN Reviewed; 99 AA.
AC Q9Z4N4; P82962;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Microcin E492;
DE Short=MccE492;
DE Flags: Precursor;
GN Name=mceA {ECO:0000303|PubMed:9864332};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 18-26.
RC STRAIN=RYC492;
RX PubMed=9864332; DOI=10.1128/jb.181.1.212-217.1999;
RA Lagos R., Villanueva J.E., Monasterio O.;
RT "Identification and properties of the genes encoding microcin E492 and its
RT immunity protein.";
RL J. Bacteriol. 181:212-217(1999).
RN [2]
RP PROTEIN SEQUENCE OF 16-99, AND MASS SPECTROMETRY.
RX PubMed=11751140; DOI=10.1128/aac.46.1.229-230.2002;
RA Pons A.-M., Zorn N., Vignon D., Delalande F., Van Dorsselaer A.,
RA Cottenceau G.;
RT "Microcin E492 is an unmodified peptide related in structure to colicin
RT V.";
RL Antimicrob. Agents Chemother. 46:229-230(2002).
RN [3]
RP PROTEIN SEQUENCE OF 16-20, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RX PubMed=12890026; DOI=10.1046/j.1365-2958.2003.03610.x;
RA Destoumieux-Garzon D., Thomas X., Santamaria M., Goulard C., Barthelemy M.,
RA Boscher B., Bessin Y., Molle G., Pons A.-M., Letellier L., Peduzzi J.,
RA Rebuffat S.;
RT "Microcin E492 antibacterial activity: evidence for a TonB-dependent inner
RT membrane permeabilization on Escherichia coli.";
RL Mol. Microbiol. 49:1031-1041(2003).
RN [4]
RP PROTEIN SEQUENCE OF 89-99, FUNCTION, MASS SPECTROMETRY, AND SIDEROPHORE
RP BINDING SITE.
RC STRAIN=RYC492;
RX PubMed=15102848; DOI=10.1074/jbc.m400228200;
RA Thomas X., Destoumieux-Garzon D., Peduzzi J., Afonso C., Blond A.,
RA Birlirakis N., Goulard C., Dubost L., Thai R., Tabet J.-C., Rebuffat S.;
RT "Siderophore peptide, a new type of post-translationally modified
RT antibacterial peptide with potent activity.";
RL J. Biol. Chem. 279:28233-28242(2004).
RN [5]
RP FUNCTION.
RX PubMed=7682973; DOI=10.1016/0014-5793(93)80096-d;
RA Lagos R., Wilkens M., Vergara C., Cecchi X., Monasterio O.;
RT "Microcin E492 forms ion channels in phospholipid bilayer membrane.";
RL FEBS Lett. 321:145-148(1993).
CC -!- FUNCTION: Channel-forming bacteriocin. Forms cation-selective channels.
CC Active on enterobacteria, with highest activity against E.coli. Not
CC active on other Gram-negative bacteria, Gram-positive bacteria or
CC fungi. The unmodified protein is active against E.coli and
CC S.enteritidis. When the siderophore ester is present at Ser-99,
CC antibacterial activity against these species is increased and activity
CC is also detected against E.cloacae and K.pneumoniae. Neutralized by its
CC immunity protein MceB (PubMed:9864332). {ECO:0000269|PubMed:12890026,
CC ECO:0000269|PubMed:15102848, ECO:0000269|PubMed:7682973,
CC ECO:0000269|PubMed:9864332}.
CC -!- SUBUNIT: Multimer. Possibly forms a homodimer or a homotrimer.
CC {ECO:0000269|PubMed:12890026}.
CC -!- PTM: The C-terminal Ser is modified by attachment to a siderophore
CC similar to enterobactin, which can bind one atom of iron. The
CC modification consists of an ester linkage of the serine carboxyl to O6
CC of a glucose which is linked by a C-glycosidic bond to the 5'-benzoyl
CC of a linear triester of N-(2,3-dihydroxybenzoyl)serine. Presence of the
CC siderophore ester increases the antibacterial activity of the protein.
CC -!- MASS SPECTROMETRY: Mass=7886.68; Mass_error=0.52; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11751140};
CC -!- MASS SPECTROMETRY: Mass=7887.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11751140};
CC -!- MASS SPECTROMETRY: Mass=7885.32; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12890026};
CC -!- MASS SPECTROMETRY: Mass=7887; Method=MALDI; Note=Ser-99 unmodified
CC form.; Evidence={ECO:0000269|PubMed:15102848};
CC -!- MASS SPECTROMETRY: Mass=8718; Method=MALDI; Note=Ser-99 modified form.;
CC Evidence={ECO:0000269|PubMed:15102848};
CC -!- SIMILARITY: Belongs to the class IIa microcin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF063590; AAD04332.2; -; Genomic_DNA.
DR RefSeq; WP_071785591.1; NZ_WYAM01000026.1.
DR PDB; 7DYR; EM; 2.28 A; A/D/G=16-99.
DR PDBsum; 7DYR; -.
DR AlphaFoldDB; Q9Z4N4; -.
DR SMR; Q9Z4N4; -.
DR TCDB; 1.C.58.1.1; the microcin e492/c24 (microcin e492) family.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Ion channel; Ion transport; Signal; Transport.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:11751140,
FT ECO:0000269|PubMed:12890026"
FT CHAIN 16..99
FT /note="Microcin E492"
FT /id="PRO_0000005677"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Serine microcin E492 siderophore ester"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:7DYR"
FT HELIX 44..66
FT /evidence="ECO:0007829|PDB:7DYR"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:7DYR"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:7DYR"
SQ SEQUENCE 99 AA; 9562 MW; FC59A5472E7D28C5 CRC64;
MREISQKDLN LAFGAGETDP NTQLLNDLGN NMAWGAALGA PGGLGSAALG AAGGALQTVG
QGLIDHGPVN VPIPVLIGPS WNGSGSGYNS ATSSSGSGS
