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Information on EC 7.2.2.7 - ABC-type Fe3+ transporter
for references in articles please use BRENDA:EC7.2.2.7
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EC Tree 7 Translocases
7.2 Catalysing the translocation of inorganic cations
7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
7.2.2.7 ABC-type Fe3+ transporter
IUBMB Comments
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains. A bacterial enzyme that interacts with a periplasmic iron-binding protein to imports Fe3+ ions into the cytoplasm.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 7.2.2.7
-
atfro2
-
lefro1
-
nramp1
-
fbpas
- nicotianamine
-
fe-deficient
-
iucabcd
-
ferric-chelate
- aerobactin
Reaction Schemes
show+
+
=
+
+
+
+
+
Fe3+-[iron-binding protein][side 1]
=
+
+
+
[iron-binding protein][side 1]
Synonyms
sitabcd, atirt1, fbpabc, leirt1, fhucbg, hfbpabc transporter, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.6.3.30
-
-
formerly
-
Fe3+-transporting ATPase
-
-
-
-
Fe3+transporting ATPase
ferrisiderophore permease system
-
-
-
-
hFbpABC transporter
IRT1
SFU
-
-
-
-
SitABCD
-
-
-
-
yfeABCD ABC-type transporter
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Fe3+-[iron-binding protein][side 1] = ADP + phosphate + Fe3+[side 2] + [iron-binding protein][side 1]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, Fe3+-transporting)
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains. A bacterial enzyme that interacts with a periplasmic iron-binding protein to imports Fe3+ ions into the cytoplasm.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: the ferrisiderophore permease system allows internalization of Fe(III) when supplied to bacterial cells as 59FeCl3 or 59Fe dicitrate via complexation to a second siderophore
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: the ferrisiderophore permease system allows internalization of Fe(III) when supplied to bacterial cells as 59FeCl3 or 59Fe dicitrate via complexation to a second siderophore
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: high specificity for Fe3+
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: shuttling of free Fe3+ through the periplasm
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: ABC7 is the causal gene of X-linked siderolastic anemia and ataxia
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: shuttling of free Fe3+ through the periplasm
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: crucial role in periplasmic transport of iron derived from human transferrin, human lactoferrin, and iron chelates
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: shuttling of free Fe3+ through the periplasm
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: SitABCD may play a major role in iron aquisition during infection, the sitABCD operon is induced under iron-deficient conditions in vitro
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: transport of iron(III)-hydroxamates
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: may be involved in either siderophore-mediated or transferrin-mediated iron uptake
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: proteins YbtP and YbtQ are members of the ABC transporter family and probably function as a heterodimer in the transport of ferri-yersiniabactin
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: cells with mutations in protein YbtP or protein YbtQ still produce yersiniabactin but are impaired in their ability to grow at 37Ā°C under iron-deficient conditions
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: involved in aquisition of organic iron. Mn2+-repression of the transcription from the yfeABCD promoter is Fur dependent
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has high selectivity for trivalent metals, including Ga3+ and Al3+, over divalent metals
Products: -
Products: -
?
additional information
?
-
-
Substrates: gene of nucleotide-binding domain expressed in Escherichia coli has intrinsic ATPase acitivity uncoupled from the iron transport process
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: shuttling of free Fe3+ through the periplasm
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: ABC7 is the causal gene of X-linked siderolastic anemia and ataxia
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: shuttling of free Fe3+ through the periplasm
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: crucial role in periplasmic transport of iron derived from human transferrin, human lactoferrin, and iron chelates
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: shuttling of free Fe3+ through the periplasm
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: SitABCD may play a major role in iron aquisition during infection, the sitABCD operon is induced under iron-deficient conditions in vitro
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: transport of iron(III)-hydroxamates
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: may be involved in either siderophore-mediated or transferrin-mediated iron uptake
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: proteins YbtP and YbtQ are members of the ABC transporter family and probably function as a heterodimer in the transport of ferri-yersiniabactin
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: cells with mutations in protein YbtP or protein YbtQ still produce yersiniabactin but are impaired in their ability to grow at 37Ā°C under iron-deficient conditions
Products: -
Products: -
?
ATP + H2O + Fe3+/out
ADP + phosphate + Fe3+/in
-
Substrates: involved in aquisition of organic iron. Mn2+-repression of the transcription from the yfeABCD promoter is Fur dependent
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe3+
-
YfuA is able to coordinate a single Fe3+ ion in an octahedral fashion, utilizing five amino acid residues
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibitory: carbonyl cyanide m-chlorophenyl hydrazone
-
amino-oxyacetic acid
-
the addition of ethylene inhibitors decreases AtIRT1 expression, ethylene could be involved in the regulation of AtIRT1 transcription
amino-oxyacetic acid
-
the addition of ethylene inhibitors decreases LeIRT1 expression, ethylene could be involved in the regulation of LeIRT1 transcription
aminoethoxyvinylglycine
-
the addition of ethylene inhibitors decreases AtIRT1 expression, ethylene could be involved in the regulation of AtIRT1 transcription
aminoethoxyvinylglycine
-
the addition of ethylene inhibitors decreases LeIRT1 expression, ethylene could be involved in the regulation of LeIRT1 transcription
Co2+
-
the addition of ethylene inhibitors decreases AtIRT1 expression, ethylene could be involved in the regulation of AtIRT1 transcription
Co2+
-
the addition of ethylene inhibitors decreases LeIRT1 expression, ethylene could be involved in the regulation of LeIRT1 transcription
silver thiosulfate
-
the addition of ethylene inhibitors decreases AtIRT1 expression, ethylene could be involved in the regulation of AtIRT1 transcription
silver thiosulfate
-
the addition of ethylene inhibitors decreases LeIRT1 expression, ethylene could be involved in the regulation of LeIRT1 transcription
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia, Hypochromic
Jasmonic acid alleviates cadmium toxicity in Arabidopsis via suppression of cadmium uptake and translocation.
Infections
Contribution of the SitABCD, MntH, and FeoB metal transporters to the virulence of avian pathogenic Escherichia coli O78 strain chi7122.
Infections
The Bartonella henselae SitABCD transporter is required for confronting oxidative stress during cell and flea invasion.
Iron Deficiencies
Differential regulation of nramp and irt metal transporter genes in wild type and iron uptake mutants of tomato.
Typhoid Fever
The Salmonella enterica serovar typhimurium divalent cation transport systems MntH and SitABCD are essential for virulence in an Nramp1G169 murine typhoid model.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene of nucleotide-binding domain expressed in Escherichia coli
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
lipoprotein anchored into cytoplasmic membrane
-
brenda
-
lipoprotein anchored into cytoplasmic membrane
-
brenda
-
the ferrisiderophore permease complex includes the periplasmic component CbrA, the integral membrane proteins CbrB and CbrC, and the ATP-binding unit CbrD
brenda
-
the ferrisiderophore permease complex includes the periplasmic component CbrA, the integral membrane proteins CbrB and CbrC, and the ATP-binding unit CbrD
-
brenda
-
protein YbtP and protein YbtQ both contain an amino-terminal membrane-spanning domain and a carboxy-terminal ATPase
brenda
-
the ABC transporter system includes a periplasmic binding protein, YfeA, an ATP-binding protein YfeB and two integral membrane proteins YfeC and YfeD
brenda
-
the ferrisiderophore permease complex includes the periplasmic component CbrA, the integral membrane proteins CbrB and CbrC, and the ATP-binding unit CbrD
-
brenda
-
the ferrisiderophore permease complex includes the periplasmic component CbrA, the integral membrane proteins CbrB and CbrC, and the ATP-binding unit CbrD
-
-
brenda
-
the ABC transporter system includes a periplasmic binding protein, YfeA, an ATP-binding protein YfeB and two integral membrane proteins YfeC and YfeD
-
brenda
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (2777 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
34000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the ferrisiderophore permease complex includes the periplasmic component CbrA, the integral membrane proteins CbrB and CbrC, and the ATP-binding unit CbrD
additional information
-
the ferrisiderophore permease complex includes the periplasmic component CbrA, the integral membrane proteins CbrB and CbrC, and the ATP-binding unit CbrD
-
additional information
-
protein YbtP and YbtQ are members of the ABC transporter family and probably function as a heterodimer in the transport of ferri-yersiniabactin. Both YbtP and YbtQ contain the permease and the ATP-binding domain fused into a single protein
additional information
-
polypeptides of 18000 Da, 29500 Da, 32000 Da and 33000 Da are encoded by the yfe locus
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
lipoprotein
-
anchored into the cytoplasmic membrane by the lipid-modified N-termini
lipoprotein
-
anchored into the cytoplasmic membrane by the lipid-modified N-termini
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E149Q
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 95%
F162L
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 104%
G155A
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 76%
G155E
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 111%
G155V
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 88%
G418A
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 38%
I174F
-
effect of permease mutaion on transport is measured, remaining transport rate 27%
I174N
-
effect of permease mutaion on transport is measured, remaining transport rate 89%
I174N/S475I
-
effect of permease mutaion on transport is measured, remaining transport rate 9%
I383N
-
effect of permease mutaion on transport is measured, remaining transport rate 100%
I497V
-
effect of permease mutaion on transport is measured, remaining transport rate 100%
L154D
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 35%
L417D
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 5%
P168A
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 116%
S146Y
-
effect of permease mutaion on transport is measured, remaining transport rate 18%
S153A
-
effect of motif 1 and 2 mutations on transport is measured, remaining transport rate 112%
S475I
-
effect of permease mutaion on transport is measured, remaining transport rate 12%
V497I
-
effect of permease mutaion on transport is measured, remaining transport rate 23%
Y196I
-
mutation in periplasmic biding protein, FbpA, greatly diminishes iron binding affinity, but has about 35% of wild-type transport activity
E164D
-
mutant in nucleotide-binding domain fbpC, 10fold reduction in specific activity
additional information
-
a Staphylococcus aureus fhuCBG deletion strain is constructed and characterized
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-FbpA is purified by cetyltrimethylammonium bromide extraction and by using a carboxymethyl Sepharose column
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
complementing plasmids are constructed, a FhuC K42N mutant is constructed
-
expression in Escherichia coli
the FbpA gene from Neisseria gonorrhoeae strain F62 is cloned for expression of the protein in Escherichia coli cells
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Khun, H.H.; Kirby, S.D.; Lee, B.C.
A Neisseria meningitidis fbpABC mutants is incapable of using nonheme iron for growth
Infect. Immun.
66
2330-2336
1998
Neisseria meningitidis
brenda
Cockayne, A.; Hill, P.J.; Powell, N.B.L.; Bishop, K.; Sims, C.; Williams, P.
Molecular cloning of a 32-kilodalton lipoprotein component of a novel iron-regulated Staphylococcus epidermidis ABC transporter
Infect. Immun.
66
3767-3774
1998
Staphylococcus aureus, Staphylococcus epidermidis
brenda
Fetherstone, J.D.; Bertolino, V.J.; Perry, R.D.
YbtP and YbtQ: two ABC transporters required for iron uptake in Yersinia pestis
Mol. Microbiol.
32
289-299
1999
Yersinia pestis
brenda
Janakiraman, A.; Slauch, J.M.
The putative iron transport system SitABCD encoded on SPI1 is required for full virulence of Salmonella typhimurium
Mol. Microbiol.
35
1146-1155
2000
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Mahe, B.; Masclaux, C.; Rauscher, L.; Enard, C.; Expert, D.
Differential expression of two siderophore-dependent iron-acquisition pathways in Erwinia chrysanthemi 3937: characterization of a novel ferrisiderophore permease of the ABC transporter family
Mol. Microbiol.
18
33-43
1995
Dickeya chrysanthemi, Dickeya chrysanthemi 3937
brenda
Allikmets, R.; Raskind, W.H.; Hutchinson, A.; Schueck, N.D.; Dean, M.; Koeller, D.M.
Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)
Hum. Mol. Genet.
8
743-749
1999
Homo sapiens
brenda
Angerer, A.; Klupp, B.; Braun, V.
Iron transporter systems of Serratia marcescens
J. Bacteriol.
174
1378-1387
1992
Serratia ficaria, Serratia liquefaciens, Serratia marcescens, Serratia marcescens W225
brenda
Zimmermann, L.; Angerer, A.; Braun, V.
Mechanistically novel iron(III) transport system in Serratia marcescens
J. Bacteriol.
171
238-243
1989
Serratia marcescens
brenda
Bearden, S.W.; Staggs, T.M.; Perry, R.D.
An ABC transporter system of Yersinia pestis allows utilization of chelated iron by Escherichia coli SAB11
J. Bacteriol.
180
1135-1147
1998
Yersinia pestis
brenda
Lau, G.H.Y.; MacGillivray, R.T.A.; Murphy, M.E.P.
Characterization of a nucleotide-binding domain associated with neisserial iron transport
J. Bacteriol.
186
3266-3269
2004
Neisseria gonorrhoeae
brenda
Anderson, D.S.; Adhikari, P.; Nowalk, A.J.; Chen, C.Y.; Mietzner, T.A.
The hFbpABC transporter from Haemophilus influenzae functions as a binding-protein-dependent ABC transporter with high specificity and affinity for ferric iron
J. Bacteriol.
186
6220-6229
2004
Haemophilus influenzae
brenda
Shouldice, S.R.; McRee, D.E.; Dougan, D.R.; Tari, L.W.; Schryvers, A.B.
Novel anion-independent iron coordination by members of a third class of bacterial periplasmic ferric ion-binding proteins
J. Biol. Chem.
280
5820-5827
2005
Serratia marcescens, Yersinia enterocolitica
brenda
Speziali, C.D.; Dale, S.E.; Henderson, J.A.; Vines, E.D.; Heinrichs, D.E.
Requirement of Staphylococcus aureus ATP-binding cassette-ATPase FhuC for iron-restricted growth and evidence that it functions with more than one iron transporter
J. Bacteriol.
188
2048-2055
2006
Staphylococcus aureus
brenda
Anderson, D.S.; Adhikari, P.; Weaver, K.D.; Crumbliss, A.L.; Mietzner, T.A.
The Haemophilus influenzae hFbpABC Fe3+ transporter: analysis of the membrane permease and development of a gallium-based screen for mutants
J. Bacteriol.
189
5130-5141
2007
Haemophilus influenzae
brenda
Weaver, K.D.; Heymann, J.J.; Mehta, A.; Roulhac, P.L.; Anderson, D.S.; Nowalk, A.J.; Adhikari, P.; Mietzner, T.A.; Fitzgerald, M.C.; Crumbliss, A.L.
Ga(3+) as a mechanistic probe in Fe(3+) transport - characterization of Ga (3+) interaction with FbpA
J. Biol. Inorg. Chem.
13
887-898
2008
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
brenda
Lucena, C.; Waters, B.M.; Romera, F.J.; Garcia, M.J.; Morales, M.; Alcantara, E.; Perez-Vicente, R.
Ethylene could influence ferric reductase, iron transporter, and H+-ATPase gene expression by affecting FER (or FER-like) gene activity
J. Exp. Bot.
57
4145-4154
2006
Arabidopsis thaliana, Solanum lycopersicum
brenda
Roehrig, S.C.; Tran, H.Q.; Spehr, V.; Gunkel, N.; Selzer, P.M.; Ullrich, H.J.
The response of Mannheimia haemolytica to iron limitation: implications for the acquisition of iron in the bovine lung
Vet. Microbiol.
121
316-329
2007
Mannheimia haemolytica, Pasteurella multocida
brenda
EXTERNAL LINKS (specific for EC-Number 7.2.2.7)
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