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InterPro: IPR003423 Outer membrane efflux protein

Protein matches Help

UniProtKB

Matches:

6709 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR003423 OMP_efflux

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02321	OEP	6709
Signatures in BioMart

InterPro Relationships Help

Children

IPR010130 Type I secretion outer membrane protein, TolC
IPR010131 RND efflux system, outer membrane lipoprotein, NodT

GO Term annotation Help

Process

GO:0006810 transport

Function

GO:0005215 transporter activity

InterPro annotation

Entry Details in BioMart

Abstract

The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm. Examples include the Escherichia coli TolC outer membrane protein, which is required for proper expression of outer membrane protein genes; the Rhizobium nodulation protein; and the Pseudomonas FusA protein, which is involved in resistance to fusaric acid.

Structural links Help

PDB - click here

SCOP: f.5.1.1

Database links Help

PANDIT: PF02321

Blocks: IPB003423

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003423

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P02930 Outer membrane protein tolC

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003423	Outer membrane efflux protein
IPR010130	Type I secretion outer membrane protein, TolC
	PDB Chain
	ModBase
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Higgins MK, Eswaran J, Edwards P, Schertler GF, Hughes C, Koronakis V. Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolC. J. Mol. Biol. 342 2004 697-702 [PubMed: 15342230] http://dx.doi.org/10.1016/j.jmb.2004.07.088
	Koronakis V, Sharff A, Koronakis E, Luisi B, Hughes C. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405 2000 914-9 [PubMed: 10879525] http://dx.doi.org/10.1038/35016007
	Johnson JM, Church GM. Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps. J. Mol. Biol. 287 1999 695-715 [PubMed: 10092468] http://dx.doi.org/10.1006/jmbi.1999.2630
	Akama H, Kanemaki M, Yoshimura M, Tsukihara T, Kashiwagi T, Yoneyama H, Narita S, Nakagawa A, Nakae T. Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J. Biol. Chem. 279 2004 52816-9 [PubMed: 15507433] http://dx.doi.org/10.1074/jbc.C400445200

InterPro 23.1