MCBA_ECOLX
ID MCBA_ECOLX Reviewed; 69 AA.
AC P05834; Q7M024;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Bacteriocin microcin B17;
DE Short=MccB17;
DE Flags: Precursor;
GN Name=mcbA;
OS Escherichia coli.
OG Plasmid IncFII pMccB17.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3329729; DOI=10.1002/prot.340010305;
RA Davagnino J., Herrero M., Furlong D., Moreno F., Kolter R.;
RT "The DNA replication inhibitor microcin B17 is a forty-three-amino-acid
RT protein containing sixty percent glycine.";
RL Proteins 1:230-238(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2644225; DOI=10.1128/jb.171.2.1126-1135.1989;
RA Genilloud O., Moreno F., Kolter R.;
RT "DNA sequence, products, and transcriptional pattern of the genes involved
RT in production of the DNA replication inhibitor microcin B17.";
RL J. Bacteriol. 171:1126-1135(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX PubMed=2835580; DOI=10.1111/j.1365-2958.1987.tb00512.x;
RA Conell N., Han Z., Moreno F., Kolter R.;
RT "An E. coli promoter induced by the cessation of growth.";
RL Mol. Microbiol. 1:195-201(1987).
RN [4]
RP PROTEIN SEQUENCE OF 27-69.
RA Bayer A., Stevanovic S., Freund S., Metzger J.W., Jung G.;
RT "Isolation and structure elucidation of the 43-peptide antibiotic microcin
RT B17.";
RL (In) Schneider C.H., Eberles A.N. (eds.);
RL Peptides 1992, pp.117-118, Escom Science Publishers, Leiden (1993).
RN [5]
RP PROTEIN SEQUENCE OF 27-38, AND POST-TRANSLATIONAL MODIFICATIONS.
RX PubMed=8183941; DOI=10.1073/pnas.91.10.4519;
RA Yorgey P., Lee J., Koerdel J., Vivas E., Warner P., Jebaratnam D.,
RA Kolter R.;
RT "Posttranslational modifications in microcin B17 define an additional class
RT of DNA gyrase inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4519-4523(1994).
RN [6]
RP FUNCTION.
RX PubMed=1846808; DOI=10.1002/j.1460-2075.1991.tb07969.x;
RA Vizan J.L., Hernandez-Chico C., del Castillo I., Moreno F.;
RT "The peptide antibiotic microcin B17 induces double-strand cleavage of DNA
RT mediated by E. coli DNA gyrase.";
RL EMBO J. 10:467-476(1991).
RN [7]
RP STRUCTURE BY NMR OF 1-26.
RX PubMed=9545435; DOI=10.1016/s1074-5521(98)90635-4;
RA Roy R.S., Kim S., Baleja J.D., Walsh C.T.;
RT "Role of the microcin B17 propeptide in substrate recognition: solution
RT structure and mutational analysis of McbA1-26.";
RL Chem. Biol. 5:217-228(1998).
CC -!- FUNCTION: This glycine-rich peptide antibiotic inhibits DNA replication
CC in many enteric bacteria, that leads to induction of the SOS repair
CC system, massive DNA degradation and cell death. B17 inhibits type II
CC topoisomerase by trapping an enzyme - DNA cleavable complex.
CC {ECO:0000269|PubMed:1846808}.
CC -!- PTM: The processed N-terminus does not resemble a typical secretion
CC signal sequence.
CC -!- PTM: Maturation of thiazole and oxazole containing antibiotics involves
CC the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl
CC of the preceding amino acid to form a thioether or ether bond, then
CC dehydration to form a double bond with the alpha-amino nitrogen.
CC Thiazoline or oxazoline rings are dehydrogenated to form thiazole or
CC oxazole rings.
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DR EMBL; M15469; AAA24141.1; -; Genomic_DNA.
DR EMBL; M24253; AAA72741.1; -; Genomic_DNA.
DR EMBL; X06417; CAA29725.1; -; Genomic_DNA.
DR PIR; A25219; MIEC77.
DR PIR; A58375; A58375.
DR RefSeq; WP_001535752.1; NZ_VRWA01000056.1.
DR PDB; 2MLP; NMR; -; A=1-26.
DR PDB; 6GOS; X-ray; 2.10 A; A=1-69.
DR PDB; 6GRG; X-ray; 2.35 A; A=1-69.
DR PDB; 6GRH; X-ray; 1.85 A; A=1-46.
DR PDBsum; 2MLP; -.
DR PDBsum; 6GOS; -.
DR PDBsum; 6GRG; -.
DR PDBsum; 6GRH; -.
DR AlphaFoldDB; P05834; -.
DR SMR; P05834; -.
DR EvolutionaryTrace; P05834; -.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; DNA replication inhibitor; Plasmid;
KW Thioether bond.
FT PROPEP 1..26
FT /evidence="ECO:0000269|PubMed:8183941, ECO:0000269|Ref.4"
FT /id="PRO_0000002772"
FT CHAIN 27..69
FT /note="Bacteriocin microcin B17"
FT /id="PRO_0000002773"
FT CROSSLNK 39..40
FT /note="Oxazole-4-carboxylic acid (Gly-Ser)"
FT /evidence="ECO:0000269|PubMed:8183941"
FT CROSSLNK 40..41
FT /note="Thiazole-4-carboxylic acid (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:8183941"
FT CROSSLNK 47..48
FT /note="Thiazole-4-carboxylic acid (Gly-Cys)"
FT /evidence="ECO:0000269|PubMed:8183941"
FT CROSSLNK 50..51
FT /note="Thiazole-4-carboxylic acid (Gly-Cys)"
FT /evidence="ECO:0000269|PubMed:8183941"
FT CROSSLNK 54..55
FT /note="Thiazole-4-carboxylic acid (Gly-Cys)"
FT /evidence="ECO:0000269|PubMed:8183941"
FT CROSSLNK 55..56
FT /note="Oxazole-4-carboxylic acid (Cys-Ser)"
FT /evidence="ECO:0000269|PubMed:8183941"
FT CROSSLNK 61..62
FT /note="Oxazole-4-carboxylic acid (Gly-Ser)"
FT /evidence="ECO:0000269|PubMed:8183941"
FT CROSSLNK 64..65
FT /note="Oxazole-4-carboxylic acid (Gly-Ser)"
FT /evidence="ECO:0000269|PubMed:8183941"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:6GRH"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:6GRH"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2MLP"
SQ SEQUENCE 69 AA; 6013 MW; 0B1D159A832638A8 CRC64;
MELKASEFGV VLSVDALKLS RQSPLGVGIG GGGGGGGGGS CGGQGGGCGG CSNGCSGGNG
GSGGSGSHI
