The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins.
about
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humansHaemophore functions revisitedGlutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpACompensating Stereochemical Changes Allow Murein Tripeptide to Be Accommodated in a Conventional Peptide-binding ProteinDelineation of the Pasteurellaceae-specific GbpA-family of glutathione-binding proteinsStructure of the nucleotide-binding domain of a dipeptide ABC transporter reveals a novel iron-sulfur cluster-binding domainHeme degrading protein HemS is involved in oxidative stress response of Bartonella henselaeHeme binding proteins of Bartonella henselae are required when undergoing oxidative stress during cell and flea invasionLactococcus lactis HemW (HemN) is a haem-binding protein with a putative role in haem traffickingHigh-throughput screening of dipeptide utilization mediated by the ABC transporter DppBCDF and its substrate-binding proteins DppA1-A5 in Pseudomonas aeruginosaA Chemical-Genomic Screen of Neglected Antibiotics Reveals Illicit Transport of Kasugamycin and Blasticidin SRapid acid treatment of Escherichia coli: transcriptomic response and recovery.Fitness of Escherichia coli during urinary tract infection requires gluconeogenesis and the TCA cycle.The dppBCDF gene cluster of Haemophilus influenzae: Role in heme utilizationComparative Genomic Analysis of the Class Epsilonproteobacteria and Proposed Reclassification to Epsilonbacteraeota (phyl. nov.).The first complete genome sequence of the class Fimbriimonadia in the phylum ArmatimonadetesMetaproteogenomic analysis of a community of sponge symbionts.Genes important for catalase activity in Enterococcus faecalis.Staphylococcus aureus FepA and FepB proteins drive heme iron utilization in Escherichia coli.Mycobacterium tuberculosis can utilize heme as an iron source.A system-level model for the microbial regulatory genomeHeme utilization by nontypeable Haemophilus influenzae is essential and dependent on Sap transporter functionCo-Inactivation of GlnR and CodY Regulators Impacts Pneumococcal Cell Wall Physiology.The Vibrio cholerae VctPDGC system transports catechol siderophores and a siderophore-free iron ligand.Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in E. coli.HasB, the Serratia marcescens TonB paralog, is specific to HasR.Permeases of the sap transporter are required for cathelicidin resistance and virulence of Haemophilus ducreyi in humansHow bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)Bacterial heme-transport proteins and their heme-coordination modes.Role and regulation of heme iron acquisition in gram-negative pathogens.Coordination of Metabolism and Virulence Factors Expression of Extraintestinal Pathogenic Escherichia coli Purified from Blood Cultures of Patients with Sepsis.Bacteria capture iron from heme by keeping tetrapyrrol skeleton intactAnalysis of the proteome of intracellular Shigella flexneri reveals pathways important for intracellular growth.Trafficking of heme and porphyrins in metazoa.Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.The iron-regulated staphylococcal lipoproteins.Analysis of the bacterial response to Ru(CO)3Cl(Glycinate) (CORM-3) and the inactivated compound identifies the role played by the ruthenium compound and reveals sulfur-containing species as a major target of CORM-3 action.Co-expression of active human cytochrome P450 1A2 and cytochrome P450 reductase on the cell surface of Escherichia coli.Heme drives hemolysis-induced susceptibility to infection via disruption of phagocyte functions.Silent mischief: bacteriophage Mu insertions contaminate products of Escherichia coli random mutagenesis performed using suicidal transposon delivery plasmids mobilized by broad-host-range RP4 conjugative machinery.
P2860
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P2860
The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins.
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
name
The housekeeping dipeptide per ...... onal peptide binding proteins.
@ast
The housekeeping dipeptide per ...... onal peptide binding proteins.
@en
type
label
The housekeeping dipeptide per ...... onal peptide binding proteins.
@ast
The housekeeping dipeptide per ...... onal peptide binding proteins.
@en
prefLabel
The housekeeping dipeptide per ...... onal peptide binding proteins.
@ast
The housekeeping dipeptide per ...... onal peptide binding proteins.
@en
P2860
P356
P1476
The housekeeping dipeptide per ...... onal peptide binding proteins.
@en
P2093
Cécile Wandersman
Sylvie Létoffé
P2860
P304
12891-12896
P356
10.1073/PNAS.0605440103
P407
P577
2006-08-11T00:00:00Z