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Information on EC 7.4.2.5 - bacterial ABC-type protein transporter

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IUBMB 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. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
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This record set is specific for:
UNIPROT: Q9M390
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
pept1, peptide transporter, pept2, seca2, abc transport, seca protein, peptide transporter 1, abcb10, seca1, seca atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
peptide-transporting ATPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transmembrane transport
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hydolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, peptide-exporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + L-Ala-L-Ala/in
ADP + phosphate + L-Ala-L-Ala/out
show the reaction diagram
K0.5 value 0.057 mM at -140 mV
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?
ATP + H2O + L-Ala-L-Asp/in
ADP + phosphate + L-Ala-L-Asp/out
show the reaction diagram
K0.5 value 0.058 mM at -140 mV
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?
ATP + H2O + L-Ala-L-Lys/in
ADP + phosphate + L-Ala-L-Lys/out
show the reaction diagram
K0.5 value 0.142 mM at -140 mV
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?
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Carbonyl cyanide m-chlorophenylhydrazone
10 mM, 26% residual activity
diethyl dicarbonate
10 mM, 0.4% residual activity
L-Phe-L-Ala
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe
L-Phe-L-Phe
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe. Phe-Ala reduces leak currents by binding to the substrate-binding site with a high apparent affinity
L-Trp-L-Ala
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe
N-ethylmaleimide
10 mM, 12% residual activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PTR1
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PTR1_ARATH
570
0
64034
Swiss-Prot
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Xenopus laevis oocyte
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hammes, U.; Meier, S.; Dietrich, D.; Ward, J.; Rentsch, D.
Functional properties of the Arabidopsis peptide transporters AtPTR1 and AtPTR5
J. Biol. Chem.
285
39710-39717
2010
Arabidopsis thaliana (Q9LFB8), Arabidopsis thaliana (Q9M390)
Manually annotated by BRENDA team