Protein Family Models

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

Date:

2024-08-14

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

ABC transporter substrate-binding protein functions as the initial receptor in the transport of substrates like fatty acids, hydrophobic amino acids, or amino acid amides, including the branched-chain amino acids leucine, isoleucine, and valine

Date:

2021-08-13

Many proteins that fold in the cytosol because a required cofactor is available there only, or because cytosolic chaperones assist in folding, or because high salt in the extracellular milieu would interfere with folding there, cannot rely on the standard general secretory (Sec) pathway for secretion across the plasma membrane. This model describes a family of predicted long, non-Sec signal sequences and signal-anchor sequences (uncleaved signal sequences). All contain a typically invariant pair of arginine residues, in a motif approximated by (S/T)-R-R-X-F-L-K, followed by a membrane-spanning hydrophobic region. The system that secretes pre-folded proteins with this motif is known as twin-arginine translocation, or TAT. Note that some variant forms, often lineage-specific ones such as the RKxFL version found in Leptospira, do occur but typically fall outside the scope of this HMM. Twin-arginine signal domains with small amino acid side chains at the -1 and -3 positions from the C-terminus of the model should be predicted to be cleaved as are Sec pathway signal sequences. The system, although far from universal in prokaryotes, is widespread in bacteria and present also in many archaea.

Date:

2019-11-27