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Links from Protein

Items: 10

1.

polysaccharide biosynthesis C-terminal domain-containing protein

This family represents the C-terminal integral membrane region of polysaccharide biosynthesis proteins. (from Pfam)

Date:
2024-08-14
Family Accession:
NF026018.5
Method:
HMM
2.

lipid II flippase MurJ

Peptidoglycan synthesis (PG) biosynthesis involves the formation of peptidoglycan precursor lipid II (undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide) on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh. MviN, renamed as MurJ, is a lipid II flippase essential for cell wall peptidoglycan synthesis [1, 2]. MurJ belongs to the MVF (mouse virulence factor) family of MOP superfamily transporters, which also includes the MATE (multidrug and toxic compound extrusion) transporter and eukaryotic OLF (oligosaccharidyl-lipid flippase) families. In addition to the canonical MOP transporter core consisting of 12 transmembrane helices (TMs), MurJ has two additional C-terminal TMs (13 and 14) of unknown function. Structural analysis indicates that the N lobe (TMs 1-6) and C lobe (TMs 7-14) are arranged in an inward-facing N-shape conformation, rather than the outward-facing V-shape conformation observed in all existing MATE transporter structures. Furthermore, a hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Mutagenesis studies, revealed a solvent-exposed cavity that is essential for function. Mutation of conserved residues (Ser17, Arg18, Arg24, Arg52, and Arg255) at the proximal site failed to complement MurJ function, consistent with the idea that these residues are important for recognizing the diphosphate and/or sugar moieties of lipid II. It has also been suggested that the chloride i. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-08-14
Family Accession:
NF015013.5
Method:
HMM
3.

MATE family efflux transporter

MATE (Multi Antimicrobial Extrusion), 2.A.66.1 in Transporter Classification Database, is a widely distributed transporter family that includes both human proteins and bacterial antibiotic resistance efflux transporters.

GO Terms:
Molecular Function:
antiporter activity (GO:0015297)
Cellular Component:
membrane (GO:0016020)
Molecular Function:
xenobiotic transmembrane transporter activity (GO:0042910)
Biological Process:
transmembrane transport (GO:0055085)
Date:
2024-08-14
Family Accession:
NF013703.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.

MATE family efflux transporter

MATE (multidrug and toxic compound extrusion) family efflux transporter functions in protecting cells against oxidative stress and bile salts and may be part of the SOS system; similar to Bacillus subtilis YoeA and YpnP

Date:
2024-08-13
Family Accession:
10192102
Method:
Sparcle
10.

MATE family efflux transporter

The Multi Antimicrobial Extrusion (MATE) Family (TC 2.A.66) The MATE family consists of probable efflux proteins including a functionally characterized multi drug efflux system from Vibrio parahaemolyticus, a putative ethionine resistance protein of Saccharomyces cerevisiae, and the functionally uncharacterized DNA damage-inducible protein F (DinF) of E. coli. These proteins have 12 probable TMS.

GO Terms:
Molecular Function:
antiporter activity (GO:0015297)
Cellular Component:
membrane (GO:0016020)
Molecular Function:
xenobiotic transmembrane transporter activity (GO:0042910)
Biological Process:
transmembrane transport (GO:0055085)
Date:
2024-06-10
Family Accession:
TIGR00797.1
Method:
HMM
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