Protein Family Models

This entry primarily matches to legume-like lectin domains found in prokaryotes. (from Pfam)

Date:

2024-08-14

This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by [1]. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as Pfam:PF05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation ([2]). Some of the proteins it is found in (e.g. Swiss:Q9RL69) are involved in methicillin resistance ([3]). The name FIVAR derives from Found In Various Architectures. [1]. 12438356. Identification of a fibronectin-binding protein from. Staphylococcus epidermidis.. Williams RJ, Henderson B, Sharp LJ, Nair SP;. Infect Immun 2002;70:6805-6810.. [2]. 14759609. Posttranslational processing of polysaccharide lyase: maturation. route for gellan lyase in Bacillus sp. GL1.. Miyake O, Kobayashi E, Nankai H, Hashimoto W, Mikami B, Murata. K;. Arch Biochem Biophys 2004;422:211-220.. [3]. 10896508. Tn551-mediated insertional inactivation of the fmtB gene. encoding a cell wall-associated protein abolishes methicillin. resistance in Staphylococcus aureus.. Komatsuzawa H, Ohta K, Sugai M, Fujiwara T, Glanzmann P,. Berger-BachiB, Suginaka H;. J Antimicrob Chemother 2000;45:421-431. (from Pfam)

Date:

2024-08-14

This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (Pfam:PF02494) and (Pfam:PF00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (Pfam:PF02639) and (Pfam:PF02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei ([1]). [1]. 12606174. Sequencing and analysis of the genome of the Whipple's disease. bacterium Tropheryma whipplei.. Bentley SD, Maiwald M, Murphy LD, Pallen MJ, Yeats CA, Dover LG,. Norbertczak HT, Besra GS, Quail MA, Harris DE, von Herbay A,. Goble A, Rutter S, Squares R, Squares S, Barrell BG, Parkhill J,. Relman DA;. Lancet 2003;361:637-644. (from Pfam)

Date:

2024-08-14

Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus. (from Pfam)

Date:

2024-08-14

The [YF]SIRKxxxGxxS type of signal peptide appears at the start of many proteins of Streptococcus, Staphylococcus, and Enterococcus, but not in other lineages such as Bacillus. Recent work in Staphylococcus aureus has shown that septal secretion (targeting to the crosswall in dividing cells) of the YSIRK-containing staphylococcal protein A depends on SecA, SecDF, and the lipoteichoic acid synthase LtaS, all of which co-purify when the motif is modified to YSIRKxxxGxxL to block processing.

Date:

2019-12-09