HtaA is an iron-regulated hemin binding protein involved in the utilization of heme iron in Corynebacterium diphtheriae.
about
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humansIsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus.The complete genome sequence of Corynebacterium pseudotuberculosis FRC41 isolated from a 12-year-old girl with necrotizing lymphadenitis reveals insights into gene-regulatory networks contributing to virulenceA combined approach for comparative exoproteome analysis of Corynebacterium pseudotuberculosis.Two coregulated efflux transporters modulate intracellular heme and protoporphyrin IX availability in Streptococcus agalactiae.The high affinity iron permease is a key virulence factor required for Rhizopus oryzae pathogenesisThe ABC transporter HrtAB confers resistance to hemin toxicity and is regulated in a hemin-dependent manner by the ChrAS two-component system in Corynebacterium diphtheriae.Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.Characterization of a hemophore-like protein from Porphyromonas gingivalis.The ClpP protease is required for the stress tolerance and biofilm formation in Actinobacillus pleuropneumoniae.Development of a Fur-dependent and tightly regulated expression system in Escherichia coli for toxic protein synthesis.Utilization of host iron sources by Corynebacterium diphtheriae: multiple hemoglobin-binding proteins are essential for the use of iron from the hemoglobin-haptoglobin complex.IsdA and IsdB antibodies protect mice against Staphylococcus aureus abscess formation and lethal challengeNon-heme-binding domains and segments of the Staphylococcus aureus IsdB protein critically contribute to the kinetics and equilibrium of heme acquisition from methemoglobin.Novel hemin binding domains in the Corynebacterium diphtheriae HtaA protein interact with hemoglobin and are critical for heme iron utilization by HtaAThe NEAT Domain-Containing Proteins of Clostridium perfringens Bind Heme.In silico identification of essential proteins in Corynebacterium pseudotuberculosis based on protein-protein interaction networksAnalysis of novel iron-regulated, surface-anchored hemin-binding proteins in Corynebacterium diphtheriaeStructural Characterization of Heme Environmental Mutants of CgHmuT that Shuttles Heme Molecules to Heme TransportersHeme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation.Transition Metals and Virulence in Bacteria.The theft of host heme by Gram-positive pathogenic bacteria.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Heme Synthesis and Acquisition in Bacterial Pathogens.Shr of group A streptococcus is a new type of composite NEAT protein involved in sequestering haem from methaemoglobinThe ChrA response regulator in Corynebacterium diphtheriae controls hemin-regulated gene expression through binding to the hmuO and hrtAB promoter regions.Control of heme homeostasis in Corynebacterium glutamicum by the two-component system HrrSA.The Corynebacterium diphtheriae iron-regulated surface protein HbpA is involved in the utilization of the Hemoglobin-Haptoglobin complex as an iron source.Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.Impact of mycolic acid deficiency on cells of Corynebacterium glutamicum ATCC13869.QseC Mediates Osmotic Stress Resistance and Biofilm Formation in Haemophilus parasuis.Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization.Iron and Zinc Regulate Expression of a Putative ABC Metal Transporter in Corynebacterium diphtheriae.Roles of B739_1343 in iron acquisition and pathogenesis in Riemerella anatipestifer CH-1 and evaluation of the RA-CH-1ΔB739_1343 mutant as an attenuated vaccine.Distinct Genomic Features Characterize Two Clades of : Proposal of Subsp. Subsp. nov. and Subsp. Subsp. nov
P2860
Q21131297-71E40D76-36DE-45E0-B5B5-C16757699088Q33687709-DF3AAFDB-153C-416C-AA4E-B116C41F296EQ33782231-89AF9A2E-3546-4A49-82B1-5718916C44B7Q33795285-D0650769-F418-4F85-A6DD-B5BEE4946AE3Q33806729-AABC0E35-BA27-4DE6-A28A-B0EEDAF41498Q34017347-13C612AE-A79E-4E41-8175-16F257875B61Q34119262-CB86FDAF-8C65-4DF1-84C4-3389900FAA53Q34309767-256A3817-9716-4162-ABE8-9C4C28D0F135Q34401001-FCDC808D-4AE2-44A1-B8CA-02D2490074DFQ34551568-138BE8F6-0C4F-423D-93FC-599E30CD3C8EQ34627454-A8FF397B-1AA5-4C79-86D3-0768FF9F03A8Q34853574-C22C24D6-1D5F-4A6C-80F7-41B1EBC2DF13Q34983585-FD7BAD37-7AE1-46A4-9E3C-085EC6256873Q35193861-6430F862-9077-445C-956D-162B69CDECBDQ35274306-49F2C62E-CEED-4979-831A-84099BC71276Q36135854-FE435FCD-D8AB-4254-ABF2-269CC9425552Q36183157-B92BF7B5-F5B0-473D-95BC-21763234A370Q36969545-08CA8E1F-EB3F-4077-9BD3-B722E382FA02Q37050520-D9E3B7A6-E88B-467E-A3CF-51472118DDABQ37090935-6BAC325A-46FF-42A4-96FF-D2F491FB31B8Q37348889-535D1FCE-7A11-41B1-9EB7-8427E5CCB59FQ37446682-40DBB1EB-2F6E-4CE4-A4C0-C134E18BB16CQ37897143-DA5FBFCC-49B3-4B6D-B4F3-890671A1F806Q38415707-9792B95E-2BE0-470B-B53F-2C2DE1D4E3FCQ38791019-3451DB84-3224-4477-938B-1CC22A7F36ABQ42398674-F72D9917-5590-4324-8561-847160C7E308Q42583913-1B3DDFBE-FD3F-421E-9113-6456146BAC22Q42706803-A859432F-B689-41C7-8B1B-016150737DEBQ47222921-706C6ADA-BDFA-4070-9A1C-49273984CA69Q48019657-E2411523-7224-4F7B-BB34-90428C203773Q48125360-00F39536-EA58-4EA2-960D-8A73E9F96158Q50317978-E26A24DC-6005-49EC-9FE3-6663CE08711BQ51465909-B36F100F-DE81-4C64-9257-E186B025D94AQ52366712-08F7351A-CE09-4B1C-922C-580511D50A97Q55311744-047B736A-01A6-4D4E-9E6F-9E4AAEDB05BFQ57922300-04B13306-9FFA-4AE1-BBDC-6B4CEE21F77C
P2860
HtaA is an iron-regulated hemin binding protein involved in the utilization of heme iron in Corynebacterium diphtheriae.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 06 February 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
HtaA is an iron-regulated hemi ...... n Corynebacterium diphtheriae.
@en
HtaA is an iron-regulated hemi ...... n Corynebacterium diphtheriae.
@nl
type
label
HtaA is an iron-regulated hemi ...... n Corynebacterium diphtheriae.
@en
HtaA is an iron-regulated hemi ...... n Corynebacterium diphtheriae.
@nl
prefLabel
HtaA is an iron-regulated hemi ...... n Corynebacterium diphtheriae.
@en
HtaA is an iron-regulated hemi ...... n Corynebacterium diphtheriae.
@nl
P2860
P356
P1476
HtaA is an iron-regulated hemi ...... n Corynebacterium diphtheriae.
@en
P2093
Courtni E Allen
Michael P Schmitt
P2860
P304
P356
10.1128/JB.01784-08
P407
P577
2009-02-06T00:00:00Z