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Items: 7

1.

Bacterial extracellular solute-binding protein, family 7

This family of proteins is involved in binding extracellular solutes for transport across the bacterial cytoplasmic membrane. This family includes Swiss:P37735, a C4-dicarboxylate-binding protein [1] and the sialic acid-binding protein SiaP. The structure of the SiaP receptor has revealed an overall topology similar to ATP binding cassette ESR (extracytoplasmic solute receptors) proteins [2]. Upon binding of sialic acid, SiaP undergoes domain closure about a hinge region and kinking of an alpha-helix hinge component [2]. [1]. 1809844. Purification, characterization and nucleotide sequence of the periplasmic C4-dicarboxylate-binding protein (DctP) from Rhodobacter capsulatus. Shaw JG, Hamblin MJ, Kelly DJ;. Mol Microbiol 1991;5:3055-3062. [2]. 16702222. Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae. Muller A, Severi E, Mulligan C, Watts AG, Kelly DJ, Wilson KS, Wilkinson AJ, Thomas GH;. J Biol Chem. 2006;281:22212-22222. [3]. 16262798. Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter. Severi E, Randle G, Kivlin P, Whitfield K, Young R, Moxon R, Kelly D, Hood D, Thomas GH;. Mol Microbiol. 2005;58:1173-1185. [4]. 20656493. Caught in a TRAP: substrate-binding proteins in secondary transport. Fischer M, Zhang QY, Hubbard RE, Thomas GH;. Trends Microbiol. 2010;18:471-478. (from Pfam)

GO Terms:
Biological Process:
transmembrane transport (GO:0055085)
Date:
2024-10-16
Family Accession:
NF015445.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.

TRAP transporter substrate-binding protein

TRAP transporter substrate-binding protein functions as the receptor subunit of a Tripartite ATP-independent Periplasmic (TRAP) transporter complex, similar to Salmonella enterica uncharacterized protein YiiZ

Date:
2018-03-02
Family Accession:
10194660
Method:
Sparcle
6.

DctP family TRAP transporter solute-binding subunit

TRAP-T (Tripartite ATP-independent Periplasmic Transporter) family proteins generally consist of three components, and these systems have so far been found in Gram-negative bacteria, Gram-postive bacteria and archaea. The best characterized example is the DctPQM system of Rhodobacter capsulatus, a C4 dicarboxylate (malate, fumarate, succinate) transporter. This model represents the DctP family, one of at least three major families of extracytoplasmic solute receptor for TRAP family transporters. Other are the SnoM family (see PF03480) and TAXI (TRAP-associated extracytoplasmic immunogenic) family.

GO Terms:
Molecular Function:
transporter activity (GO:0005215)
Cellular Component:
tripartite ATP-independent periplasmic transporter complex (GO:0031317)
Biological Process:
transmembrane transport (GO:0055085)
Date:
2024-06-27
Family Accession:
TIGR00787.1
Method:
HMM
7.

TRAP transporter substrate-binding protein DctP

Proteins of this family are members of the superfamily of Tripartite ATP-independent Periplasmic Transporter (TRAP-T). They transport hydrophobic substrates, usually lipoprotein.

Gene:
dctP
GO Terms:
Biological Process:
transmembrane transport (GO:0055085)
Date:
2022-03-28
Family Accession:
NF037995.1
Method:
HMM
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