MCCC7_ECOLX
ID MCCC7_ECOLX Reviewed; 7 AA.
AC Q47505;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 53.
DE RecName: Full=Microcin C7;
DE Short=MccC7;
DE AltName: Full=Microcin C51;
DE Short=McC;
DE Short=MccC51;
DE Short=Microcin C;
GN Name=mccA {ECO:0000312|EMBL:CAA40808.1};
OS Escherichia coli.
OG Plasmid pMccC7 {ECO:0000312|EMBL:CAA40808.1}.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=2861788; DOI=10.1128/aac.27.5.791;
RA Garcia-Bustos J.F., Pezzi N., Mendez E.;
RT "Structure and mode of action of microcin 7, an antibacterial peptide
RT produced by Escherichia coli.";
RL Antimicrob. Agents Chemother. 27:791-797(1985).
RN [2] {ECO:0000312|PIR:S45311}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8183363; DOI=10.1038/369281a0;
RA Gonzalez-Pastor J.E., San Millan J.L., Moreno F.;
RT "The smallest known gene.";
RL Nature 369:281-281(1994).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, FORMYLATION AT MET-1, AND
RP PHOSPHORAMIDE AT ASN-7.
RX PubMed=7835418; DOI=10.1016/0014-5793(94)01345-2;
RA Metlitskaya A.Z., Katrukha G.S., Shashkov A.S., Zaitsev D.A., Egorov T.A.,
RA Khmel I.A.;
RT "Structure of microcin C51, a new antibiotic with a broad spectrum of
RT activity.";
RL FEBS Lett. 357:235-238(1995).
RN [4] {ECO:0000312|EMBL:CAA40808.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8522520; DOI=10.1128/jb.177.24.7131-7140.1995;
RA Gonzalez-Pastor J.E., San Millan J.L., Castilla M.A., Moreno F.;
RT "Structure and organization of plasmid genes required to produce the
RT translation inhibitor microcin C7.";
RL J. Bacteriol. 177:7131-7140(1995).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=16574659; DOI=10.1074/jbc.m513174200;
RA Metlitskaya A.Z., Kazakov T., Kommer A., Pavlova O., Praetorius-Ibba M.,
RA Ibba M., Krasheninnikov I., Kolb V., Khmel I.A., Severinov K.;
RT "Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic
RT microcin C.";
RL J. Biol. Chem. 281:18033-18042(2006).
RN [6] {ECO:0000305}
RP REVIEW.
RX PubMed=17827970; DOI=10.1159/000104748;
RA Duquesne S., Petit V., Peduzzi J., Rebuffat S.;
RT "Structural and functional diversity of microcins, gene-encoded
RT antibacterial peptides from enterobacteria.";
RL J. Mol. Microbiol. Biotechnol. 13:200-209(2007).
RN [7] {ECO:0000305}
RP REVIEW.
RX PubMed=17711420; DOI=10.1111/j.1365-2958.2007.05874.x;
RA Severinov K., Semenova E., Kazakov A., Kazakov T., Gelfand M.S.;
RT "Low-molecular-weight post-translationally modified microcins.";
RL Mol. Microbiol. 65:1380-1394(2007).
RN [8] {ECO:0000305}
RP FUNCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=18223070; DOI=10.1128/jb.01956-07;
RA Kazakov T., Vondenhoff G.H., Datsenko K.A., Novikova M., Metlitskaya A.Z.,
RA Wanner B.L., Severinov K.;
RT "Escherichia coli peptidase A, B, or N can process translation inhibitor
RT microcin C.";
RL J. Bacteriol. 190:2607-2610(2008).
RN [9] {ECO:0000305}
RP STRUCTURE BY NMR, FUNCTION, MASS SPECTROMETRY, FORMYLATION AT MET-1, AND
RP PHOSPHORAMIDE AT ASN-7.
RX PubMed=7559516; DOI=10.1074/jbc.270.40.23520;
RA Guijarro J.I., Gonzalez-Pastor J.E., Baleux F., San Millan J.L.,
RA Castilla M.A., Rico M., Moreno F., Delepierre M.;
RT "Chemical structure and translation inhibition studies of the antibiotic
RT microcin C7.";
RL J. Biol. Chem. 270:23520-23532(1995).
CC -!- FUNCTION: Antibacterial peptide, active against enterobacteria
CC including species of Klebsiella, Salmonella, Shigella, Yersinia and
CC Proteus, and strains of E.coli. Inhibits protein translation by
CC blocking aspartyl-tRNA synthetase function and inhibiting production of
CC aminoacetylated tRNA-Asp. {ECO:0000269|PubMed:16574659,
CC ECO:0000269|PubMed:17827970, ECO:0000269|PubMed:18223070,
CC ECO:0000269|PubMed:2861788, ECO:0000269|PubMed:7559516}.
CC -!- INTERACTION:
CC Q47505; Q47506: mccB; NbExp=8; IntAct=EBI-7035319, EBI-7035293;
CC -!- PTM: The peptide moiety allows entry into the bacterial cell, where it
CC undergoes proteolytic cleavage to release the aspartyl adenylate
CC analog, which is responsible for aspartyl-tRNA synthetase inhibition.
CC Can be processed by the non-specific oligopeptidases PepA, PepB and
CC PepN. {ECO:0000269|PubMed:16574659, ECO:0000269|PubMed:17711420,
CC ECO:0000269|PubMed:17827970, ECO:0000269|PubMed:18223070}.
CC -!- MASS SPECTROMETRY: Mass=1177; Mass_error=1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7559516, ECO:0000269|PubMed:7835418};
CC -!- MASS SPECTROMETRY: Mass=1177.5; Method=Plasma desorption;
CC Evidence={ECO:0000269|PubMed:7559516, ECO:0000269|PubMed:7835418};
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; X57583; CAA40808.1; -; Genomic_DNA.
DR PIR; S45311; S45311.
DR PDB; 3H5R; X-ray; 2.10 A; E/F/G/H=1-7.
DR PDB; 3H9G; X-ray; 2.20 A; E/F/G/H=1-7.
DR PDB; 3H9J; X-ray; 2.30 A; E/F/G/H=1-7.
DR PDB; 3H9Q; X-ray; 2.63 A; E/F/G/H=1-7.
DR PDBsum; 3H5R; -.
DR PDBsum; 3H9G; -.
DR PDBsum; 3H9J; -.
DR PDBsum; 3H9Q; -.
DR SMR; Q47505; -.
DR IntAct; Q47505; 1.
DR MINT; Q47505; -.
DR EvolutionaryTrace; Q47505; -.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Formylation; Phosphoprotein; Plasmid.
FT PEPTIDE 1..7
FT /note="Microcin C7"
FT /evidence="ECO:0000269|PubMed:2861788,
FT ECO:0000269|PubMed:8183363"
FT /id="PRO_0000341532"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:7559516,
FT ECO:0000269|PubMed:7835418"
FT MOD_RES 7
FT /note="Aspartic acid 1-[(3-aminopropyl)(5'-
FT adenosyl)phosphono]amide"
FT /evidence="ECO:0000269|PubMed:7559516,
FT ECO:0000269|PubMed:7835418"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3H9G"
SQ SEQUENCE 7 AA; 763 MW; 644DD44861B406F0 CRC64;
MRTGNAN
