Protein Family Models

This domain is found at the elbow of internalin surface proteins, used by the bacteria to invade mammalian cells. This domain has an Ig-like fold [1]. [1]. 23958637. Structure of internalin InlK from the human pathogen Listeria monocytogenes. Neves D, Job V, Dortet L, Cossart P, Dessen A;. J Mol Biol. 2013;425:4520-4529. (from Pfam)

Date:

2024-10-16

This domain is found in bacterial cell surface proteins that interact with mucins. The archetypal member of this family is the Mub-R5 B1 domain [1]. This domain has a beta-grasp fold [1]. [1]. 19758995. Crystal structure of a mucus-binding protein repeat reveals an unexpected functional immunoglobulin binding activity. MacKenzie DA, Tailford LE, Hemmings AM, Juge N;. J Biol Chem. 2009;284:32444-32453. (from Pfam)

Date:

2024-11-04

This entry represents a bacterial immunoglobulin-like domain found in bacterial proteins, including Pesticidal crystal protein Cry22Aa from Bacillus thuringiensis, a protein with a toxic effect on several insect larvae and Chitinase 60 from Moritella marina (Swiss:B1VBB0), responsible for degradation of krill chitin. Paper describing PDB structure 4hmc. [1]. 23633591. Structure of a complete four-domain chitinase from Moritella marina, a marine psychrophilic bacterium. Malecki PH, Raczynska JE, Vorgias CE, Rypniewski W;. Acta Crystallogr D Biol Crystallogr. 2013;69:821-829. Paper describing PDB structure 4mb3. [2]. 24598737. Crystal structures of substrate-bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution. Malecki PH, Vorgias CE, Petoukhov MV, Svergun DI, Rypniewski W;. Acta Crystallogr D Biol Crystallogr. 2014;70:676-684. Paper describing PDB structure 5fq3. [3]. 28077872. Structural basis for nutrient acquisition by dominant members of the human gut microbiota. Glenwright AJ, Pothula KR, Bhamidimarri SP, Chorev DS, Basle A, Firbank SJ, Zheng H, Robinson CV, Winterhalter M, Kleinekathofer U, Bolam DN, van den Berg B;. Nature. 2017;541:407-411. Paper describing PDB structure 5kdj. [4]. 28096352. Recognition of protein-linked glycans as a determinant of peptidase activity. Noach I, Ficko-Blean E, Pluvinage B, Stuart C, Jenkins ML, Brochu D, Buenbrazo N, Wakarchuk W, Burke JE, Gilbert M, Boraston AB;. Proc Natl Acad Sci U S A. 2017;114:E679. (from Pfam)

Date:

2024-10-16

These are small, all beta strand domains, structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats (LRR), significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier [1],[2] [3]. [1]. 11575932. Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T, Chakraborty T, Wehland J, Domann E, Heinz DW;. J Mol Biol 2001;312:783-794. [2]. 12526809. Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin. Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW;. Cell 2002;111:825-836. [3]. 15003459. Folding and stability of the leucine-rich repeat domain of internalin B from Listeri monocytogenes. Freiberg A, Machner MP, Pfeil W, Schubert WD, Heinz DW, Seckler R;. J Mol Biol 2004;337:453-461. (from Pfam)

Date:

2024-10-16

The MucBP (MUCin-Binding Protein) domain is found in a wide variety of bacterial proteins, in several repeats. The domain is found in bacterial peptidoglycan bound proteins and is often found in conjunction with Pfam:PF00746 and Pfam:PF00560. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

This model describes a tandem repeat about 80 amino acids in length per repeat, found in at least 12 different surface-exposed proteins of the pathogen Listeria monocytogenes, and in particular found 10 times in tandem in the surface protein LapB, for which the repeat is named.

Date:

2020-10-26

This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region.

Date:

2021-04-27

Members of this orthologous family, including lmo0171 from genome NC_003210.1, are class 1 (LPXTG-type) internalins.

Date:

2018-01-16