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| Rhizoferrin |
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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. ... |
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| Rhizoferrin |
|
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. ... |
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| Rhizoferrin |
|
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. ... |
|
| Rhizoferrin |
|
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. ... |
|
| Rhizoferrin |
|
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. ... |
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Hgp
(Hemoglobin-binding protein) |
|
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. ... |
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Hgp
(Hemoglobin-binding protein) |
|
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. ... |
|
Hgp
(Hemoglobin-binding protein) |
|
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. ... |
|
Hgp
(Hemoglobin-binding protein) |
|
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. ... |
|
Hgp
(Hemoglobin-binding protein) |
|
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. ... |
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