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Information on EC 7.4.2.5 - bacterial ABC-type protein transporter

for references in articles please use BRENDA:EC7.4.2.5
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EC Tree
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: Q63424
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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 + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
show the reaction diagram
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
S15A2_RAT
729
0
81320
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20100
2 * 20100, isoform PEPT2, X-ray crystallography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 20100, isoform PEPT2, X-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
extracellular domain from isoform PepT2, sitting drop vapor diffusion method, using 0.2 M (NH4)3 citrate (pH 5.8) and 21% PEG (w/v) 3350
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beale, J.H.; Parker, J.L.; Samsudin, F.; Barrett, A.L.; Senan, A.; Bird, L.E.; Scott, D.; Owens, R.J.; Sansom, M.S.; Tucker, S.J.; Meredith, D.; Fowler, P.W.; Newstead, S.
Crystal structures of the extracellular domain from PepT1 and PepT2 provide novel insights into mammalian peptide transport
Structure
23
1889-1899
2015
Rattus norvegicus (Q63424), Mus musculus (Q9JIP7)
Manually annotated by BRENDA team