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Information on EC 7.6.2.11 - ABC-type polyamine transporter
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7.6.2.11 ABC-type polyamine transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports putrescine and spermidine. In Escherichia coli the enzyme imports spermidine preferentially.
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Word Map
- 7.6.2.11
- spermine
- difluoromethylornithine
-
cho-mg
- alpha-difluoromethylornithine
- antizyme
-
bisguanylhydrazone
- homospermidine
- epipodophyllotoxin
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
+
+
=
+
+
+
+
+
polyamine-[polyamine-binding protein][side 1]
=
+
+
polyamine[side 2]
+
[polyamine-binding protein][side 1]
Synonyms
polyamine transport system, potabcd, sapbcdf, spermidine/putrescine-binding periplasmic protein, polyamine abc transporter, putrescine exporter, spermidine/putrescine abc transporter permease, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
polyamine transport system
polyamine-transporting ATPase
-
-
-
-
PotA
potABCD
potADB
PotB
PotD
putrescine export system ATP-binding protein
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
putrescine export system permease protein
putrescine exporter
SapA
SapB
SapBCDF
spermidine/putrescine ABC transporter permease
spermidine/putrescine import ATP-binding protein
putrescine export system permease protein
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
putrescine export system permease protein
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
-
spermidine/putrescine ABC transporter permease
Streptococcus suis SC-19
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
-
-
spermidine/putrescine import ATP-binding protein
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
Q8YM92; Q8YM93; Q8YM94
-
-
spermidine/putrescine import ATP-binding protein
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
Q8YM92; Q8YM93; Q8YM94
-
-
spermidine/putrescine import ATP-binding protein
Streptococcus suis SC-19
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + polyamine-[polyamine-binding protein][side 1] = ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, polyamine-importing)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports putrescine and spermidine. In Escherichia coli the enzyme imports spermidine preferentially.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
ATP + H2O + spermine-[polyamine-binding protein][side 1]
ADP + phosphate + spermine[side 2] + [polyamine-binding protein][side 1]
spermidine/out + ADP + H2O
spermidine/in + ?
-
the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
-
-
?
spermidine/out + CTP + H2O
spermidine/in + CDP + phosphate
-
the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
-
?
spermidine/out + GTP + H2O
spermidine/in + GDP + phosphate
-
the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
-
?
spermidine/out + UTP + H2O
spermidine/in + UDP + phosphate
-
the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
-
?
spermine/out + ATP + H2O
spermine/in + ADP + phosphate
-
two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Streptococcus suis SC-19
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + putrescine/out
ADP + phosphate + putrescine/in
-
putrescine-ornithine antiporter, encoded by the gene potE
-
-
r
ATP + H2O + putrescine/out
ADP + phosphate + putrescine/in
-
the putrescine-specific system, encoded by the genes potABCD, is specific for this polyamine
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
-
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
Streptococcus suis SC-19
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
-
-
-
?
ATP + H2O + spermidine/out
ADP + phosphate + spermidine/in
-
the spermidine-preferential system, encoded by the genes potFGHI, can transport both spermidine and putrescine
-
-
?
ATP + H2O + spermidine/out
ADP + phosphate + spermidine/in
-
the spermidine-preferential system, encoded by the genes potFGHI, can trasport both spermidine and putrescine
-
-
?
ATP + H2O + spermine-[polyamine-binding protein][side 1]
ADP + phosphate + spermine[side 2] + [polyamine-binding protein][side 1]
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
-
-
-
?
ATP + H2O + spermine-[polyamine-binding protein][side 1]
ADP + phosphate + spermine[side 2] + [polyamine-binding protein][side 1]
Streptococcus suis SC-19
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
-
-
-
?
putrescine/out + ATP + H2O
putrescine/in + ADP + phosphate
-
two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system
-
?
putrescine/out + ATP + H2O
putrescine/in + ADP + phosphate
-
higher affinity for spermidine than for putrescine
-
?
spermidine/out + ATP + H2O
spermidine/in + ADP + phosphate
-
-
-
-
?
spermidine/out + ATP + H2O
spermidine/in + ADP + phosphate
-
two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system.The nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
-
-
?
additional information
?
-
-
PotA protein and PotD protein are absolutely necessary for spermidine uptake in conjugation with the two channel forming proteins PotB and PotC
-
-
?
additional information
?
-
-
the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229
-
-
?
additional information
?
-
-
the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229
-
-
?
additional information
?
-
-
the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229
-
-
?
additional information
?
-
-
the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229
-
-
?
additional information
?
-
-
PotA protein is involved in the energy-coupling step
-
-
?
additional information
?
-
-
Pot D is the primary receptor of the polyamine transport system, which regulates the polyamine content in E. coli
-
-
?
additional information
?
-
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
PotD binding assays and ATPase activity assays of PotA are performed. A preference for extracellular polyamines in Streptococcus suis is identified as spermidine, spermine, putrescine in descending order, the uptake is competitive among the three
-
-
?
additional information
?
-
-
PotD binding assays and ATPase activity assays of PotA are performed. A preference for extracellular polyamines in Streptococcus suis is identified as spermidine, spermine, putrescine in descending order, the uptake is competitive among the three
-
-
?
additional information
?
-
Streptococcus suis SC-19
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
PotD binding assays and ATPase activity assays of PotA are performed. A preference for extracellular polyamines in Streptococcus suis is identified as spermidine, spermine, putrescine in descending order, the uptake is competitive among the three
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
additional information
?
-
-
Pot D is the primary receptor of the polyamine transport system, which regulates the polyamine content in E. coli
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
Q8YM92; Q8YM93; Q8YM94
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
reaction of spermine and ATP is enhanced by formation of an anti oriented ternary complex containing ATP, Mg2+ and spermine
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
spermidine
-
non competitive to ATP, acting as a feedback inhibitor of the spermidine transport
additional information
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
putrescine does not inhibit the ATPase activity of PotA
-
additional information
-
putrescine does not inhibit the ATPase activity of PotA
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Involvement of the polyamine transport system in cellular uptake of the radioprotectants WR-1065 and WR-33278.
Carcinoma, Hepatocellular
Antitumor effects and preliminary systemic toxicity of ANISpm in vivo and in vitro.
Hypertension
ATP13A3 is a major component of the enigmatic mammalian polyamine transport system.
Infections
Functional characterization of murB-potABCD operon for polyamine uptake and peptidoglycan synthesis in Streptococcus suis.
Infections
Polyamine transport in human promyelocytic leukemia cells and polymorphonuclear leukocytes.
Leukemia
Aliphatic chain length specificity of the polyamine transport system in ascites L1210 leukemia cells.
Melanoma
Harnessing the polyamine transport system to treat BRAF inhibitor-resistant melanoma.
Melanoma, Experimental
Paraquat is not accumulated in B16 tumor cells by the polyamine transport system.
Meningitis, Bacterial
Computational approaches to identify common subunit vaccine candidates against bacterial meningitis.
Neoplasms
(99m)Tc-HYNIC-spermine for imaging polyamine transport system-positive tumours: preclinical evaluation.
Neoplasms
(Z)-1,4-diamino-2-butene as a vector of boron, fluorine, or iodine for cancer therapy and imaging: synthesis and biological evaluation.
Neoplasms
A fluorescent biomarker of the polyamine transport system to select patients with AML for F14512 treatment.
Neoplasms
Activity of the polyamine-vectorized anti-cancer drug F14512 against pediatric glioma and neuroblastoma cell lines.
Neoplasms
Analysis of the in vitro and in vivo effects of photodynamic therapy on prostate cancer by using new photosensitizers, protoporphyrin IX-polyamine derivatives.
Neoplasms
Ant 4,4, a polyamine-anthracene conjugate, induces cell death and recovery in human promyelogenous leukemia cells (HL-60).
Neoplasms
Clickable polyamine derivatives as chemical probes for the polyamine transport system.
Neoplasms
Development of Polyamine Transport Ligands with Improved Metabolic Stability and Selectivity against Specific Human Cancers.
Neoplasms
Evaluation of Polyamine Transport Inhibitors in a Drosophila Epithelial Model Suggests the Existence of Multiple Transport Systems.
Neoplasms
F14512, a polyamine-vectorized anti-cancer drug, currently in clinical trials exhibits a marked preclinical anti-leukemic activity.
Neoplasms
F14512, a potent antitumor agent targeting topoisomerase II vectored into cancer cells via the polyamine transport system.
Neoplasms
Interactions between the Etoposide Derivative F14512 and Human Type II Topoisomerases: Implications for the C4 Spermine Moiety in Promoting Enzyme-Mediated DNA Cleavage.
Neoplasms
N-Benzylpolyamines as vectors of boron and fluorine for cancer therapy and imaging: synthesis and biological evaluation.
Neoplasms
Phase I dose-escalation study of F14512, a polyamine-vectorized topoisomerase II inhibitor, in patients with platinum-refractory or resistant ovarian cancer.
Neoplasms
Polyamine transport system-targeted nanometric micelles assembled from epipodophyllotoxin-amphiphiles.
Neoplasms
Polyamine-blocking therapy reverses immunosuppression in the tumor microenvironment.
Neoplasms
Polyamine-containing etoposide derivatives as poisons of human type II topoisomerases: Differential effects on topoisomerase II? and II?.
Neoplasms
Polyaminoquinoline iron chelators for vectorization of antiproliferative agents: design, synthesis, and validation.
Neoplasms
Preclinical activity of F14512, designed to target tumors expressing an active polyamine transport system.
Neoplasms
Quilamine HQ1-44, an iron chelator vectorized toward tumor cells by the polyamine transport system, inhibits HCT116 tumor growth without adverse effect.
Neoplasms
Regulation by survivin of cancer cell death induced by F14512, a polyamine-containing inhibitor of DNA topoisomerase II.
Neoplasms
Synthesis and biological evaluation of chalcone-polyamine conjugates as novel vectorized agents in colorectal and prostate cancer chemotherapy.
Neoplasms
Synthesis and biological properties of Quilamines II, new iron chelators with antiproliferative activities.
Neoplasms
Targeting the Polyamine Transport System with Benzazepine- and Azepine-Polyamine Conjugates ().
Neoplasms
The antitumor drug F14512 enhances cisplatin and ionizing radiation effects in head and neck squamous carcinoma cell lines.
Neoplasms
The polyamine analog PG11047 potentiates the antitumor activity of cisplatin and bevacizumab in preclinical models of lung and prostate cancer.
Neuroblastoma
Characterization of the polyamine transport system in mouse neuroblastoma cells. Effects of sodium and system A amino acids.
Ovarian Neoplasms
Phase I dose-escalation study of F14512, a polyamine-vectorized topoisomerase II inhibitor, in patients with platinum-refractory or resistant ovarian cancer.
Prostatic Neoplasms
Selective exclusion by the polyamine transporter as a mechanism for differential radioprotection of amifostine derivatives.
Pulmonary Arterial Hypertension
ATP13A3 is a major component of the enigmatic mammalian polyamine transport system.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.385
ATP
-
ATPase activity of the potA subunit in the spermidine-preferential system
additional information
additional information
-
dissociation constant of spermidine and putrescine of the spermidine-preferential uptake system in presence of 1 mM Mg2+ and 100 mM K+ at pH 7.5 are 0.0032 mM and 0.1 mM
-
additional information
additional information
-
PotD binds spermidine with a 0.0032 mM dissociation constant
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.4
-
ATPase activity of the potA subunit in the spermidine-preferential system
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes sapABCDF encoding probable ABC transporter periplasmic-binding protein SapA, putrescine export system permease proteins SapB and SapC, putrescine export system ATP-binding proteins SapD and SapF
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
UniProt
brenda
genes all5044, all5043, and all5042, encoding spermidine/putrescine import ATP-binding protein PotA, polyamine-binding protein of polyamine ABC transporter PotD, and permease protein of polyamine ABC transporter PotB; i.e. Anabaena sp. PCC 7120
Q8YM92; Q8YM93; Q8YM94
UniProt
brenda
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
genes all5044, all5043, and all5042, encoding spermidine/putrescine import ATP-binding protein PotA, polyamine-binding protein of polyamine ABC transporter PotD, and permease protein of polyamine ABC transporter PotB; i.e. Anabaena sp. PCC 7120
Q8YM92; Q8YM93; Q8YM94
UniProt
brenda
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
genes all5044, all5043, and all5042, encoding spermidine/putrescine import ATP-binding protein PotA, polyamine-binding protein of polyamine ABC transporter PotD, and permease protein of polyamine ABC transporter PotB; i.e. Anabaena sp. PCC 7120
Q8YM92; Q8YM93; Q8YM94
UniProt
brenda
genes potA, potB, potC, and potD encoding spermidine/putrescine import ATP-binding protein PotA, spermidine/putrescine ABC transporter permease PotB, spermidine/putrescine ABC transporter permease protein PotC, and spermidine/putrescine-binding periplasmic protein PotD; isolated from a diseased pig in Sichuan province of China
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
UniProt
brenda
Streptococcus suis SC-19
genes potA, potB, potC, and potD encoding spermidine/putrescine import ATP-binding protein PotA, spermidine/putrescine ABC transporter permease PotB, spermidine/putrescine ABC transporter permease protein PotC, and spermidine/putrescine-binding periplasmic protein PotD; isolated from a diseased pig in Sichuan province of China
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
UniProt
brenda
genes sapABCDF encoding probable ABC transporter periplasmic-binding protein SapA, putrescine export system permease proteins SapB and SapC, putrescine export system ATP-binding proteins SapD and SapF
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
UniProt
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
Escherichia coli can grow on putrescine as a sole carbon or nitrogen source
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Escherichia coli can grow on putrescine as a sole carbon or nitrogen source
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
PotB and PotC contain six putative transmembrane segments linked by hydrophobic segments of variable length
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
SapABCDF is specifically distributed within gamma-proteobacteria
evolution
-
SapABCDF is specifically distributed within gamma-proteobacteria
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malfunction
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t
malfunction
Q8YM92; Q8YM93; Q8YM94
inactivation of the gene cluster potADB, encoding a polyamine ABC transporter disrupted diazotrophic growth, corroborates the importance of polyamine homeostasis in Nostoc sp. PCC 7120
malfunction
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
PotA deletion disrupts normal peptidoglycan synthesis and hampers cell elongation. In contrast to the wild-type, the mutant DELTApotA exhibits elongated chain length and abnormal cell division morphology. Phenotypic changes are attributed to be the upregulation of genes involved in peptidoglycan (PG) synthesis and hydrolysis in DELTApotA. Cultivation of strain SC-19 in presence of excessive spermidine or spermine displays attenuated growth
malfunction
Streptococcus suis SC-19
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PotA deletion disrupts normal peptidoglycan synthesis and hampers cell elongation. In contrast to the wild-type, the mutant DELTApotA exhibits elongated chain length and abnormal cell division morphology. Phenotypic changes are attributed to be the upregulation of genes involved in peptidoglycan (PG) synthesis and hydrolysis in DELTApotA. Cultivation of strain SC-19 in presence of excessive spermidine or spermine displays attenuated growth
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malfunction
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
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inactivation of the gene cluster potADB, encoding a polyamine ABC transporter disrupted diazotrophic growth, corroborates the importance of polyamine homeostasis in Nostoc sp. PCC 7120
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malfunction
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
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inactivation of the gene cluster potADB, encoding a polyamine ABC transporter disrupted diazotrophic growth, corroborates the importance of polyamine homeostasis in Nostoc sp. PCC 7120
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malfunction
-
deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t
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metabolism
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
the enzyme complex SapBCDF exports putrescine from Escherichia coli cells to the culture supernatant, which is the natural function of the SapBCDF proteins, while PotABCD is a spermidine transporter of the ABC transporter family that takes up putrescine with lower affinity. Mechanism of polyamine export from bacterial cells to the intestinal lumen. PuuP is a putrescine importer dependent on proton-motive force and is indispensable when Escherichia coli grows on putrescine as a sole carbon or nitrogen source. PlaP is a proton-dependent putrescine importer that is important when Escherichia coli exhibits surface motility. PotE is responsible for both excretion and uptake of putrescine. PotE is a proton-dependent putrescine importer at neutral pH, but at acidic pH PotE is a putrescine-ornithine antiporter
metabolism
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the enzyme complex SapBCDF exports putrescine from Escherichia coli cells to the culture supernatant, which is the natural function of the SapBCDF proteins, while PotABCD is a spermidine transporter of the ABC transporter family that takes up putrescine with lower affinity. Mechanism of polyamine export from bacterial cells to the intestinal lumen. PuuP is a putrescine importer dependent on proton-motive force and is indispensable when Escherichia coli grows on putrescine as a sole carbon or nitrogen source. PlaP is a proton-dependent putrescine importer that is important when Escherichia coli exhibits surface motility. PotE is responsible for both excretion and uptake of putrescine. PotE is a proton-dependent putrescine importer at neutral pH, but at acidic pH PotE is a putrescine-ornithine antiporter
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physiological function
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
the natural function of the SapBCDF enzyme complex is the export of putrescine, Escherichia coli can grow on putrescine as a sole carbon or nitrogen source
physiological function
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
the polyamine transport system PotABCD in Streptococcus suis can uptake polyamines preferably spermidine and spermine. Spermidine and putrescine have been found to be constituents of the cell wall peptidoglycan, these molecules maintain the integrity of the cell surface structure and normal cell growth. The known de novo synthesis pathway is not observed in strain SC-19 according to the genome of the strain. Regulatory roles of polyamine on polyamine transport and peptidoglycan (PG) synthesis. Polyamines function not only as feedback regulators of PotA by inhibiting PotA activity but also as regulators on potABCD and genes involved in PG synthesis. The binding of high-concentration spermidine to PotA decreases the ATPase activity and inhibits polyamine transport. PotD can downregulate the transcription of the potABCD operon. Thus, both receptor and ligand can function as feedback regulators of polyamine transport
physiological function
Streptococcus suis SC-19
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the polyamine transport system PotABCD in Streptococcus suis can uptake polyamines preferably spermidine and spermine. Spermidine and putrescine have been found to be constituents of the cell wall peptidoglycan, these molecules maintain the integrity of the cell surface structure and normal cell growth. The known de novo synthesis pathway is not observed in strain SC-19 according to the genome of the strain. Regulatory roles of polyamine on polyamine transport and peptidoglycan (PG) synthesis. Polyamines function not only as feedback regulators of PotA by inhibiting PotA activity but also as regulators on potABCD and genes involved in PG synthesis. The binding of high-concentration spermidine to PotA decreases the ATPase activity and inhibits polyamine transport. PotD can downregulate the transcription of the potABCD operon. Thus, both receptor and ligand can function as feedback regulators of polyamine transport
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physiological function
-
the natural function of the SapBCDF enzyme complex is the export of putrescine, Escherichia coli can grow on putrescine as a sole carbon or nitrogen source
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additional information
Q8YM92; Q8YM93; Q8YM94
ABC uptake transporters typically comprise one periplasmic solute-binding protein (SBP), two integral membrane proteins (transmembrane domains [TMD]) and two nucleotide-binding domains (NBD) that hydrolyze ATP in the cytoplasm, in which the TMD and NBD may be homo- or heterodimers
additional information
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, also involved in peptidoglycan synthesis
additional information
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the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, also involved in peptidoglycan synthesis
additional information
Streptococcus suis SC-19
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the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, also involved in peptidoglycan synthesis
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additional information
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
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ABC uptake transporters typically comprise one periplasmic solute-binding protein (SBP), two integral membrane proteins (transmembrane domains [TMD]) and two nucleotide-binding domains (NBD) that hydrolyze ATP in the cytoplasm, in which the TMD and NBD may be homo- or heterodimers
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additional information
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
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ABC uptake transporters typically comprise one periplasmic solute-binding protein (SBP), two integral membrane proteins (transmembrane domains [TMD]) and two nucleotide-binding domains (NBD) that hydrolyze ATP in the cytoplasm, in which the TMD and NBD may be homo- or heterodimers
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
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? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
31000
35000
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? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
38000
-
? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
39000
-
? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
43000
-
? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
45000
-
? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
31000
-
? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
31000
-
? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
additional information
?
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
x * 49000, recombinant His-tagged PotA, SDS-PAGE, x * 38000, recombinant His-tagged PotD, SDS-PAGE
?
Streptococcus suis SC-19
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x * 49000, recombinant His-tagged PotA, SDS-PAGE, x * 38000, recombinant His-tagged PotD, SDS-PAGE
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oligomer
-
? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
oligomer
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? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the PotD protein consists of two domains with an alterating beta-alpha-beta topology
additional information
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the spermidine-preferential uptake system consists of 4 proteins, that are all necessary for spermidine uptake: PotA, PotB, PotC and PotD. The calculated molecular weights are 43000 Da for PotA, 31000 Da for PotB, 29000 Da for PotC and 39000 Da for PotD. The putrescine-uptake system consists of the 4 proteins: PotF, PotG, PotH and PotI. All 4 proteins are necessary for maximal putrescine transport. PotF is a 38000 Da putrescine binding protein, PotG is a 45000 Da membrane-associated ATPase, PotH and PotI are 31000-35000 Da channel-forming proteins
additional information
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PotA protein and PotD protein are absolutely necessary for spermidine uptake in conjugation with the two channel forming proteins PotB and PotC
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C54T
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mutated PotA protein loses both ATPase and spermidine uptake activity
additional information
additional information
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construction of mutants truncated at the carboxylic terminal domain of the potA subunit, these mutants have reduced activity
additional information
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
generation of several sap gene deletion mutants, phenotypes, overview. Deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t
additional information
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generation of several sap gene deletion mutants, phenotypes, overview. Deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t
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additional information
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82
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inactivation of the gene cluster potADB
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additional information
Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576
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inactivation of the gene cluster potADB
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PotA and PotD from Escherichia coli strain BL21(DE3) by nickel affinity chromataography
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cluster potADB, or genes all5044, all5043, and all5042, encoding a polyamine ABC transporter, DELTAall5044-all5042::C.S3
Q8YM92; Q8YM93; Q8YM94
potABCD operon, genetic organization analysis, only one operon encoding a polyamine transport system (potABCD) is identified in the Streptococcus suis genome, sequence comparisons, the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, quantitative real-time PCR expression analysis of murB-potABCD operon in both wild-type and DELTApotA mutant strains. Recombinant expression of genes potA and potD, encoding PotA and PotD, in Escherichia coli strain BL21(DE3) as His-tagged proteins
A0A142UTH4; A0A0K2E5X6; G7SFQ8; A0A116LEI2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sugiyama, S.; Matsuo, Y.; Maenaka, K.; Vassylyev, D.G.; Matsushima, M.; Kashiwagi, K.; Igarashi, K.; Mirikawa, K.
The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding
Protein Sci.
5
1984-1990
1996
Escherichia coli
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Kashiwagi, K.; Miyamoto, S.; Nukui, E.; Kobayashi, H.; Igarashi, K.
Functions of PotA and PotD proteins in spermidine-preferential uptake system in Escherichia coli
J. Biol. Chem.
268
19358-19363
1993
Escherichia coli
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Meksuriyen, D.; Fukuchi-Shimogori, T.; Tomitori, H.; Kashiwagi, K.; Toida, T.; Imanari, T.; Kawai, G.; Igarashi, K.
Formation of a complex containing ATP, Mg2+, and spermine. Structural evidence and biological significance
J. Biol. Chem.
273
30939-30944
1998
Escherichia coli
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Kashiwagi, K.; Endo, H.; Kobayashi, H.; Igarashi, K.
Spermidine-preferential uptake system in Escherichia coli. ATP hydrolysis by PotA protein and its association with membranes
J. Biol. Chem.
270
25377-25382
1995
Escherichia coli
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Sugiyama, S.; Vassylyev, D.G.; Matsushima, M.; Kashiwagi, K.; Igarashi, K.; Morikawa, K.
Crystal structure of potD, the primary receptor of the poylamine transport system in Escherichia coli
J. Biol. Chem.
271
9519-9525
1996
Escherichia coli
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Kashiwagi, K.; Pistocchi, R.; Shibuya, S.; Sugiyama, S; Morikawa, K.; Igarashi, K.
Spermidine-preferential uptake system in Escherichia coli. Identification of amino acids involved in polyamine binding in PotD proteins
J. Biol. Chem.
271
12205-12208
1996
Escherichia coli
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Igarashi, K.; Kashiwagi, K.
Polyamine transport in bacteria and yeast
Biochem. J.
344
633-642
1999
Archaeoglobus fulgidus, Borreliella burgdorferi, Escherichia coli, Haemophilus influenzae, Mycoplasma genitalium, Mycoplasma pneumoniae, Treponema pallidum
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Kashiwagi, K.; Innami, A.; Zenda, R.; Tomitori, H.; Igarashi, K.
The ATPase activity and the functional domain of PotA, a component of the sermidine-preferential uptake system in Escherichia coli
J. Biol. Chem.
277
24212-24219
2002
Escherichia coli
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Igarashi, K.; Ito, K.; Kashiwagi, K.
Polyamine uptake systems in Escherichia coli
Res. Microbiol.
152
271-278
2001
Escherichia coli
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Sugiyama, Y.; Nakamura, A.; Matsumoto, M.; Kanbe, A.; Sakanaka, M.; Higashi, K.; Igarashi, K.; Katayama, T.; Suzuki, H.; Kurihara, S.
A novel putrescine exporter SapBCDF of Escherichia coli
J. Biol. Chem.
291
26343-26351
2016
Escherichia coli (Q47622 AND P0AGH3 AND P0AGH5 AND P0AAH4 AND P0AAH8), Escherichia coli MG1655 (Q47622 AND P0AGH3 AND P0AGH5 AND P0AAH4 AND P0AAH8)
-
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Liu, W.; Tan, M.; Zhang, C.; Xu, Z.; Li, L.; Zhou, R.
Functional characterization of murB-potABCD operon for polyamine uptake and peptidoglycan synthesis in Streptococcus suis
Microbiol. Res.
207
177-187
2018
Streptococcus suis (A0A142UTH4 AND A0A0K2E5X6 AND G7SFQ8 AND A0A116LEI2), Streptococcus suis, Streptococcus suis SC-19 (A0A142UTH4 AND A0A0K2E5X6 AND G7SFQ8 AND A0A116LEI2)
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Burnat, M.; Li, B.; Kim, S.; Michael, A.; Flores, E.
Homospermidine biosynthesis in the cyanobacterium Anabaena requires a deoxyhypusine synthase homologue and is essential for normal diazotrophic growth
Mol. Microbiol.
109
763-780
2018
Nostoc sp. PCC 7120 = FACHB-418 (Q8YM92 AND Q8YM93 AND Q8YM94), Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576 (Q8YM92 AND Q8YM93 AND Q8YM94), Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82 (Q8YM92 AND Q8YM93 AND Q8YM94)
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EXTERNAL LINKS (specific for EC-Number 7.6.2.11)
Transporter Classification Database (TCDB): 3.A.1.11.10, 3.A.1.11.1, 3.A.1.11.7, 3.A.1.11.8, 3.A.1.11.3, 3.A.1.20.1, 3.A.1.11.4
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