U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

entB [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946178, updated on 11-Sep-2024

Summary

Go to the top of the page Help
Official Symbol
entB
Primary source
ECOCYC:EG10260
Locus tag
b0595
See related
ASAP:ABE-0002052
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
ECK0588; entG
Summary
Recent gel filtration data suggest that EntB may be a trimer not a pentamer. [More information is available at EcoCyc: EG10260].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Sequence:
NC_000913.3 (627694..628551)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene isochorismate synthase EntC Neighboring gene 2,3-dihydroxybenzoate-AMP ligase Neighboring gene 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase Neighboring gene proofreading thioesterase in enterobactin biosynthesis Neighboring gene pyruvate transporter CstA

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Structural and functional investigation of the intermolecular interaction between NRPS adenylation and carrier protein domains. Sundlov JA, et al. Chem Biol, 2012 Feb 24. PMID 22365602, Free PMC Article
  2. EntG activity of Escherichia coli enterobactin synthetase. Staab JF, et al. J Bacteriol, 1990 Nov. PMID 2172214, Free PMC Article
  3. Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase. Rusnak F, et al. Biochemistry, 1990 Feb 13. PMID 2139796
  4. Ligand-induced conformational rearrangements promote interaction between the Escherichia coli enterobactin biosynthetic proteins EntE and EntB. Khalil S, et al. J Mol Biol, 2009 Oct 30. PMID 19699210
  5. Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain. Drake EJ, et al. Chem Biol, 2006 Apr. PMID 16632253

See all (27) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The aryl carrier protein (ArCP) domain of EntB interacts specifically with EntH to help with the proofreading role for EntH during biosynthesis of enterobactin.
    Title: The hotdog thioesterase EntH (YbdB) plays a role in vivo in optimal enterobactin biosynthesis by interacting with the ArCP domain of EntB.
  2. crystal structure of the EntB protein that contains an N-terminal isochorismate lyase domain that functions in the synthesis of 2,3-dihydroxybenzoate and a C-terminal carrier protein domain
    Title: Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain.
Submit: New GeneRIF Correction

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables 2,3-dihydroxybenzoate-serine ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 2,3-dihydroxybenzoate-serine ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables isochorismatase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables isochorismatase activity IEA
Inferred from Electronic Annotation
more info
  
enables ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables magnesium ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables phosphopantetheine binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables transferase activity, transferring alkyl or aryl (other than methyl) groups IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
involved_in enterobactin biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in enterobactin biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
enterobactin synthase component B
NP_415127.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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
    627694..628551
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415127.1 enterobactin synthase component B [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415127.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7RNN6
    Conserved Domains (2) summary
    COG1535
    Location:1 → 215
    EntB; Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism]
    COG3433
    Location:216 → 285
    DhbB2; Aryl carrier domain [Secondary metabolites biosynthesis, transport and catabolism]
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.