SMART: Pfam domain Peripla_BP

Peripla_BP_2

PFAM accession number:	PF01497
Interpro abstract (IPR002491):	ATP binding cassette (ABC) transporters are a ubiquitous family of importer and exporter proteins that consist of two alpha-helical transmembrane (TM) domains, which form a translocation pathway, and two cytoplasmic ABC domains, which power the transport reaction through binding and hydrolysis of ATP. In addition most bacterial importers employs a periplasmic substrate-binding protein (PBP) that delivers the ligand to the extracellular gate of the TM domains. These proteins bind their substrates selectively and with high affinity, which is thought to ensure the specificity of the transport reaction. Binding proteins in Gram-negative bacteria are present within the periplasm, whereas those in Gram-positive bacteria are tethered to the cell membrane via the acylation of a cysteine residue that is an integral component of a lipoprotein signal sequence. The cobalamin (vitamin B12) and the iron transport systems share many common attributes and probably evolved from the same origin [ (PUBMED:12475936) (PUBMED:14514690) (PUBMED:2651410) ]. The structure of the periplasmic-binding domain is composed of two subdomains, each consisting of a central beta-sheet and surrounding alpha-helices, linked by a rigid alpha-helix. The substrate binding site is located in a cleft between the two alpha/beta subdomains [ (PUBMED:12468528) ]. Some protein known to contain an iron siderophore/cobalamin periplasmic- binding domain are listed below: Escherichia coli vitamin B12 transport protein btuF. It is the periplasmic binding protein for the vitamin B12 transporter btuCD. Escherichia coli ferrichrome-binding periplasmic protein (fhuD). It binds iron(III)-hydroxamates. Staphylococcus aureus ferric hydroxamate receptor 2 (fhuD2). Escherichia coli ferrienterobactin-binding periplasmic protein fepB. It binds ferrienterobactin; part of the binding-protein-dependent transport system for uptake of ferrienterobactin. Vibrio cholerae periplasmic binding protein (viuP). Escherichia coli iron(III) dicitrate-binding periplasmic protein (fecB). It binds citrate-dependent iron(III); part of the binding-protein-dependent transport system for uptake of citrate-dependent iron(III). Erwinia chrysanthemi achromobactin-binding periplasmic protein (cbrA). It binds citrate-or chloride-dependent iron(III); part of the binding-protein-dependent transport system cbrABCD for uptake of the siderophore achromobactin. Yersinia pestis hemin-binding periplasmic protein (hmuT).

PFAM accession number:

PF01497

Interpro abstract (IPR002491):

ATP binding cassette (ABC) transporters are a ubiquitous family of importer and exporter proteins that consist of two alpha-helical transmembrane (TM) domains, which form a translocation pathway, and two cytoplasmic ABC domains, which power the transport reaction through binding and hydrolysis of ATP. In addition most bacterial importers employs a periplasmic substrate-binding protein (PBP) that delivers the ligand to the extracellular gate of the TM domains. These proteins bind their substrates selectively and with high affinity, which is thought to ensure the specificity of the transport reaction. Binding proteins in Gram-negative bacteria are present within the periplasm, whereas those in Gram-positive bacteria are tethered to the cell membrane via the acylation of a cysteine residue that is an integral component of a lipoprotein signal sequence. The cobalamin (vitamin B12) and the iron transport systems share many common attributes and probably evolved from the same origin [ (PUBMED:12475936) (PUBMED:14514690) (PUBMED:2651410) ].

The structure of the periplasmic-binding domain is composed of two subdomains, each consisting of a central beta-sheet and surrounding alpha-helices, linked by a rigid alpha-helix. The substrate binding site is located in a cleft between the two alpha/beta subdomains [ (PUBMED:12468528) ].

Some protein known to contain an iron siderophore/cobalamin periplasmic- binding domain are listed below:

Escherichia coli vitamin B12 transport protein btuF. It is the periplasmic binding protein for the vitamin B12 transporter btuCD.
Escherichia coli ferrichrome-binding periplasmic protein (fhuD). It binds iron(III)-hydroxamates.
Staphylococcus aureus ferric hydroxamate receptor 2 (fhuD2).
Escherichia coli ferrienterobactin-binding periplasmic protein fepB. It binds ferrienterobactin; part of the binding-protein-dependent transport system for uptake of ferrienterobactin.
Vibrio cholerae periplasmic binding protein (viuP).
Escherichia coli iron(III) dicitrate-binding periplasmic protein (fecB). It binds citrate-dependent iron(III); part of the binding-protein-dependent transport system for uptake of citrate-dependent iron(III).
Erwinia chrysanthemi achromobactin-binding periplasmic protein (cbrA). It binds citrate-or chloride-dependent iron(III); part of the binding-protein-dependent transport system cbrABCD for uptake of the siderophore achromobactin.
Yersinia pestis hemin-binding periplasmic protein (hmuT).

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peripla_BP_2