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prc tail-specific protease [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946096, updated on 3-Dec-2024

Summary

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Official Symbol
prc
Official Full Name
tail-specific protease
Primary source
ECOCYC:EG10760
Locus tag
b1830
See related
ASAP:ABE-0006090
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1829; tsp
Summary
Penicillin-binding protein PBP3 is a typical Prc substrate. [More information is available at EcoGene: EG10760]. Tail-specific protease (Tsp) is an ATP-independent periplasmic protease responsible for processing and degradation of a number of proteins . [More information is available at EcoCyc: EG10760].
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Genomic context

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Sequence:
NC_000913.3 (1912768..1914816, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative transporter YebQ Neighboring gene protease HtpX Neighboring gene RNA chaperone ProQ Neighboring gene free methionine-(R)-sulfoxide reductase

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Structural Basis for the Differential Regulatory Roles of the PDZ Domain in C-Terminal Processing Proteases. Chueh CK, et al. mBio, 2019 Aug 6. PMID 31387902, Free PMC Article
  2. Multiple antibiotic susceptibility associated with inactivation of the prc gene. Seoane A, et al. J Bacteriol, 1992 Dec. PMID 1447154, Free PMC Article
  3. Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini. Silber KR, et al. Proc Natl Acad Sci U S A, 1992 Jan 1. PMID 1729701, Free PMC Article
  4. Carboxy-terminal determinants of intracellular protein degradation. Parsell DA, et al. Genes Dev, 1990 Feb. PMID 2186965
  5. Genetic analyses of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli. Hara H, et al. J Bacteriol, 1989 Nov. PMID 2681145, Free PMC Article

See all (33) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. We demonstrated for the first time that Prc is essential for full Extraintestinal pathogenic E. coli (ExPEC) virulence in urinary tract infections. Our results collectively support the idea that Prc is essential for bacterial envelope integrity, thus explaining how Prc deficiency results in an attenuated ExPEC.
    Title: The role of the bacterial protease Prc in the uropathogenesis of extraintestinal pathogenic Escherichia coli.
  2. In Prc, a hydrophobic substrate sensor engages substrate binding to the PDZ domain and triggers a structural remodeling to align the active-site residues.
    Title: Structural Basis for the Differential Regulatory Roles of the PDZ Domain in C-Terminal Processing Proteases.
  3. A proteolytic system comprising the periplasmic PDZ-protease Prc and the lipoprotein adaptor NlpI contributes to Peptidoglycan (PG) enlargement.
    Title: Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc.
  4. ProQ and Prc deficiencies lowered the ProP activity of bacteria cultivated at moderate salinity by approximately 70% and 30%, respectively, but did not affect other osmoregulatory functions.
    Title: Salinity-dependent impacts of ProQ, Prc, and Spr deficiencies on Escherichia coli cell structure.
  5. N-terminus verified by Edman degradation on mature peptide
    Title: Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini.
Submit: New GeneRIF Correction

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables endopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables endopeptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables endopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables serine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables serine-type peptidase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within protein catabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within proteolysis IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within proteolysis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within response to antibiotic IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in signal transduction IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
is_active_in outer membrane-bounded periplasmic space IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
tail-specific protease
NP_416344.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1912768..1914816 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416344.1 tail-specific protease [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416344.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A6M9WVC8
    Conserved Domains (1) summary
    PRK11186
    Location:4 → 674
    PRK11186; carboxy terminal-processing peptidase
Nucleotide Protein
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