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Links from Protein

Items: 7

1.

substrate-binding domain-containing protein

This family includes bacterial extracellular solute-binding proteins. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024921.5
Method:
HMM
2.

extracellular solute-binding protein

This family also includes the bacterial extracellular solute-binding protein family POTD/POTF. [1]. 2002054. The 2.3-A resolution structure of the maltose- or. maltodextrin-binding protein, a primary receptor of bacterial. active transport and chemotaxis.. Spurlino JC, Lu GY, Quiocho FA;. J Biol Chem 1991;266:5202-5219.. [2]. 9360608. Structure of Haemophilus influenzae Fe(+3)-binding protein. reveals convergent evolution within a superfamily.. Bruns CM, Nowalk AJ, Arvai AS, McTigue MA, Vaughan KG, Mietzner. TA, McRee DE;. Nat Struct Biol 1997;4:919-924.. [3]. 9651355. Crystal structure and mutational analysis of the Escherichia. coli putrescine receptor. Structural basis for substrate. specificity.. Vassylyev DG, Tomitori H, Kashiwagi K, Morikawa K, Igarashi K;. J Biol Chem 1998;273:17604-17609.. [4]. 8336670. Structural, functional, and evolutionary relationships among. extracellular solute-binding receptors of bacteria.. Tam R, Saier MH Jr;. Microbiol Rev 1993;57:320-346. (from Pfam)

Date:
2024-08-14
Family Accession:
NF013697.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
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.

molybdate ABC transporter substrate-binding protein

The model describes the molybdate ABC transporter periplasmic binding protein in bacteria and archae. Several of the periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. It has been shown experimentally by radioactive labeling that ModA represent hydrophylioc periplasmic-binding protein in gram-negative organisms and its counterpart in gram-positive organisms is a lipoprotein. The other components of the system include the ModB, an integral membrane protein and ModC the ATP-binding subunit. Invariably almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains.

Gene:
modA
GO Terms:
Molecular Function:
ABC-type molybdate transporter activity (GO:0015412)
Biological Process:
molybdate ion transport (GO:0015689)
Cellular Component:
outer membrane-bounded periplasmic space (GO:0030288)
Molecular Function:
molybdate ion binding (GO:0030973)
Cellular Component:
ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing (GO:0055052)
Date:
2024-07-12
Family Accession:
TIGR01256.1
Method:
HMM
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