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VF category: Iron uptake (total 761 related VFs in database, current show from 21 to 30)
 
VF Bacteria Brief description
Acinetobactin
Acinetobacter
(A. baumannii ACICU)
An iron-chelating molecule composed of equimolar quantities of 2,3-dihydroxybenzoic acid (DHBA), L-threonine, and N-hydroxyhistamine. ...
Hal
(Heme-acquisition leucine-rich repeat protein)
Bacillus
(B. anthracis str. Sterne)
Includes an N-terminal near-iron transporter (NEAT) domain, several internal leucine-rich repeat (LRR) regions, and a C-terminal sortase-like cell wall anchor. ...
IlsA
(Iron-regulated leucine rich surface protein type A)
Bacillus
(B. cereus ATCC 10987)
The three conserved domains: NEAT (NEAr iron Transporter), LRR (Leucine-Rich Repeat) and SLH (Surface Layer Homology). Specifically expressed in the insect hemocoel and under iron-depleted conditions. ...
Petrobactin
Bacillus
(B. anthracis str. Sterne)
Catechol-based siderophore. The biosynthetic pathway for petrobactin (the asb operon), the petrobactin-iron complex receptor (FhuA), import permeases (FpuB/FatC/FatD), ATPases (FpuC/FatE), and the petrobactin exporter (ApeX). ...
FupA
(Fe utilization protein A)
Francisella
(F. tularensis subsp. tularensis SCHU S4)
FupA and FslE are paralogs belonging to a family of proteins unique to Francisella. Both FupA and FslE fold as β- barrels in the outer membrane with amino-terminal periplasmic domains. ...
Rhizoferrin
Francisella
(F. tularensis subsp. tularensis SCHU S4)
Siderophore-mediated Iron acquisition. Siderophore biosynthesis involves enzymes FslA and FslC, while export across the inner membrane is mediated by FslB. Uptake of the rhizoferrin- ferric iron complex is effected by the siderophore receptor FslE in the outer membrane in a TonB-independent process, and FslD is responsible for uptake across the inner membrane. ...
Hgp
(Hemoglobin-binding protein)
Haemophilus
(H. influenzae Rd KW20)
H. influenzae has an absolute requirement for exogenously supplied heme for aerobic growth. Most of the pathway converting δ-aminolevulinic acid to heme is lost. So H. influenzae has derived several mechanism to use host heme-hemopexin, hemoglobin-haptoglobin as sources of heme iron for growth. Three hemoglobin- and hemoglobin-haptoglobin binding protein genes, hgpA, hgpB, and hgpC, contain lengths of tetrameric CCAA repeats. ...
HhuA
(Hemoglobin:haptoglobin complexes binding protein)
Haemophilus
(H. influenzae TN106)
Similar to HgpA, mediates binding of both hemoglobin:haptoglobin complexes and free hemoglobin. ...
HitABC
Haemophilus
(H. influenzae Rd KW20)
hitA encodes a periplasmic ferric-binding protein A (FbpA), a high-affinity iron-binding protein belonging to the transferrin superfamily. hitB encodes a cytoplasmic permease. hitC encodes ATP-binding protein. ...
HxuABC
Haemophilus
(H. influenzae Rd KW20)
HxuA is a 100-kDa protein that binds heme-hemopexin, HxuB is a 60 kDa protein involved in the release of HxuA from the cell surface into the medium, HxuC is involved in the transport of heme within the cell. ...
   


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