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Protein

Microcin J25

Gene

mcjA

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). May inhibit transcription by binding in RNAP secondary channel and blocking nucleotide substrates access to the catalytic center. Exhibits potent bacteriocidal activity against a range of Enterobacteriaceae, including several pathogenic E.coli, Salmonella and Shigella strains. Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. Induces bacterial filamentation in susceptible cells in a non-SOS-dependent way, but this phenotype may result from impaired transcription of genes coding for cell division proteins.3 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin

Protein family/group databases

TCDBi9.A.52.1.1. the microcin j25 (microsin j25) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Microcin J25
Short name:
MccJ25
Gene namesi
Name:mcjA
Encoded oniPlasmid pTUC1000 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000027741 – 371 PublicationAdd BLAST37
PeptideiPRO_000000277538 – 58Microcin J25Add BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki38 ↔ 45Isoglutamyl glycine isopeptide (Gly-Glu)

Keywords - PTMi

Isopeptide bond

Expressioni

Inductioni

At the onset of stationary growth phase.

Interactioni

Protein-protein interaction databases

DIPiDIP-60856N.

Structurei

Secondary structure

158
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 44Combined sources6
Beta strandi48 – 51Combined sources4
Beta strandi55 – 57Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PP5NMR-A38-58[»]
1Q71NMR-A38-58[»]
1S7PNMR-A38-47[»]
B48-58[»]
2MMTNMR-A38-58[»]
2MMWNMR-A38-58[»]
4CU4X-ray2.30B38-58[»]
SMRiQ9X2V7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X2V7.

Sequencei

Sequence statusi: Complete.

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

Q9X2V7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKHFHFNKL SSGKKNNVPS PAKGVIQIKK SASQLTKGGA GHVPEYFVGI

GTPISFYG
Length:58
Mass (Da):6,200
Last modified:November 1, 1999 - v1
Checksum:iA9F4393C8EAAC8FA
GO

Mass spectrometryi

Molecular mass is 2107.0 Da from positions 38 - 58. Determined by ESI. 1 Publication
Molecular mass is 2106.0 Da from positions 38 - 58. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061787 Genomic DNA. Translation: AAD28494.1.
RefSeqiWP_001513516.1. NZ_MCBU01000092.1.
YP_009071192.1. NC_025179.1.

Genome annotation databases

GeneIDi20493264.

Cross-referencesi

Web resourcesi

Protein Spotlight

Entanglement - Issue 72 of July 2006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061787 Genomic DNA. Translation: AAD28494.1.
RefSeqiWP_001513516.1. NZ_MCBU01000092.1.
YP_009071192.1. NC_025179.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PP5NMR-A38-58[»]
1Q71NMR-A38-58[»]
1S7PNMR-A38-47[»]
B48-58[»]
2MMTNMR-A38-58[»]
2MMWNMR-A38-58[»]
4CU4X-ray2.30B38-58[»]
SMRiQ9X2V7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60856N.

Protein family/group databases

TCDBi9.A.52.1.1. the microcin j25 (microsin j25) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi20493264.

Miscellaneous databases

EvolutionaryTraceiQ9X2V7.

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiMCJA_ECOLX
AccessioniPrimary (citable) accession number: Q9X2V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to have a head-to-tail cyclic structure, but actually has a threaded side chain-to-backbone ring structure that is penetrated by the C-terminal tail in a noose-like motif.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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.