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Protein

Bacteriocin microcin B17

Gene

mcbA

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This glycine-rich peptide antibiotic inhibits DNA replication in many enteric bacteria, that leads to induction of the SOS repair system, massive DNA degradation and cell death. B17 inhibits type II topoisomerase by trapping an enzyme - DNA cleavable complex.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin, DNA replication inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Bacteriocin microcin B17
Short name:
MccB17
Gene namesi
Name:mcbA
Encoded oniPlasmid IncFII pMccB170 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 26262 PublicationsPRO_0000002772Add
BLAST
Chaini27 – 6943Bacteriocin microcin B17PRO_0000002773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki39 ↔ 40Oxazole-4-carboxylic acid (Gly-Ser)1 Publication
Cross-linki40 ↔ 41Thiazole-4-carboxylic acid (Ser-Cys)1 Publication
Cross-linki47 ↔ 48Thiazole-4-carboxylic acid (Gly-Cys)1 Publication
Cross-linki50 ↔ 51Thiazole-4-carboxylic acid (Gly-Cys)1 Publication
Cross-linki54 ↔ 55Thiazole-4-carboxylic acid (Gly-Cys)1 Publication
Cross-linki55 ↔ 56Oxazole-4-carboxylic acid (Cys-Ser)1 Publication
Cross-linki61 ↔ 62Oxazole-4-carboxylic acid (Gly-Ser)1 Publication
Cross-linki64 ↔ 65Oxazole-4-carboxylic acid (Gly-Ser)1 Publication

Post-translational modificationi

The processed N-terminus does not resemble a typical secretion signal sequence.
Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline rings are dehydrogenated to form thiazole or oxazole rings.

Keywords - PTMi

Thioether bond

Miscellaneous databases

PMAP-CutDBP05834.

Structurei

Secondary structure

1
69
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 158Combined sources
Helixi18 – 214Combined sources
Beta strandi22 – 243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MLPNMR-A1-26[»]
ProteinModelPortaliP05834.
SMRiP05834. Positions 1-26.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05834.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi26 – 3914Poly-GlyAdd
BLAST

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELKASEFGV VLSVDALKLS RQSPLGVGIG GGGGGGGGGS CGGQGGGCGG
60
CSNGCSGGNG GSGGSGSHI
Length:69
Mass (Da):6,013
Last modified:November 1, 1988 - v1
Checksum:i0B1D159A832638A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15469 Genomic DNA. Translation: AAA24141.1.
M24253 Genomic DNA. Translation: AAA72741.1.
X06417 Genomic DNA. Translation: CAA29725.1.
PIRiA25219. MIEC77.
A58375.
RefSeqiWP_001535752.1. NZ_LRWC01000091.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15469 Genomic DNA. Translation: AAA24141.1.
M24253 Genomic DNA. Translation: AAA72741.1.
X06417 Genomic DNA. Translation: CAA29725.1.
PIRiA25219. MIEC77.
A58375.
RefSeqiWP_001535752.1. NZ_LRWC01000091.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MLPNMR-A1-26[»]
ProteinModelPortaliP05834.
SMRiP05834. Positions 1-26.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP05834.
PMAP-CutDBP05834.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "The DNA replication inhibitor microcin B17 is a forty-three-amino-acid protein containing sixty percent glycine."
    Davagnino J., Herrero M., Furlong D., Moreno F., Kolter R.
    Proteins 1:230-238(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "DNA sequence, products, and transcriptional pattern of the genes involved in production of the DNA replication inhibitor microcin B17."
    Genilloud O., Moreno F., Kolter R.
    J. Bacteriol. 171:1126-1135(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "An E. coli promoter induced by the cessation of growth."
    Conell N., Han Z., Moreno F., Kolter R.
    Mol. Microbiol. 1:195-201(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
  4. "Isolation and structure elucidation of the 43-peptide antibiotic microcin B17."
    Bayer A., Stevanovic S., Freund S., Metzger J.W., Jung G.
    (In) Schneider C.H., Eberles A.N. (eds.); Peptides 1992, pp.117-118, Escom Science Publishers, Leiden (1993)
    Cited for: PROTEIN SEQUENCE OF 27-69.
  5. "Posttranslational modifications in microcin B17 define an additional class of DNA gyrase inhibitor."
    Yorgey P., Lee J., Koerdel J., Vivas E., Warner P., Jebaratnam D., Kolter R.
    Proc. Natl. Acad. Sci. U.S.A. 91:4519-4523(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-38, POST-TRANSLATIONAL MODIFICATIONS.
  6. "The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase."
    Vizan J.L., Hernandez-Chico C., del Castillo I., Moreno F.
    EMBO J. 10:467-476(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Role of the microcin B17 propeptide in substrate recognition: solution structure and mutational analysis of McbA1-26."
    Roy R.S., Kim S., Baleja J.D., Walsh C.T.
    Chem. Biol. 5:217-228(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-26.

Entry informationi

Entry nameiMCBA_ECOLX
AccessioniPrimary (citable) accession number: P05834
Secondary accession number(s): Q7M024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 11, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.