Protein Family Models

This entry represents the C-terminal trimerisation domain of bacteriophage T4 gp5. This domain associates to form a triple-stranded beta-helix that forms an equilateral triangular prism, which acts as a membrane-puncturing needle [1-2]. The interior of the beta-helix has an increased hydrophobicity toward the C terminus. The middle part of the helix has a pore, enriched with polar and charged side chains. Paper describing PDB structure 1k28. [1]. 11823865. Structure of the cell-puncturing device of bacteriophage T4. Kanamaru S, Leiman PG, Kostyuchenko VA, Chipman PR, Mesyanzhinov VV, Arisaka F, Rossmann MG;. Nature 2002;415:553-557. Paper describing PDB structure 1pdl. [2]. 12923574. Three-dimensional structure of bacteriophage T4 baseplate. Kostyuchenko VA, Leiman PG, Chipman PR, Kanamaru S, van Raaij MJ, Arisaka F, Mesyanzhinov VV, Rossmann MG;. Nat Struct Biol. 2003;10:688-693. Paper describing PDB structure 1wth. [3]. 15701513. Control of bacteriophage T4 tail lysozyme activity during the infection process. Kanamaru S, Ishiwata Y, Suzuki T, Rossmann MG, Arisaka F;. J Mol Biol. 2005;346:1013-1020. Paper describing PDB structure 2z6b. [4]. 18098245. Molecular design of heteroprotein assemblies providing a bionanocup as a chemical reactor. Koshiyama T, Yokoi N, Ueno T, Kanamaru S, Nagano S, Shiro Y, Arisaka F, Watanabe Y;. Small. 2008;4:50-54. Paper describing PDB structure 3a1m. [5]. 20661999. Construction of robust bio-nanotubes using the controlled self-assembly of component proteins of bacteriophage T4. Yokoi N, Inaba H, Terauchi M, Stieg AZ, Sanghamitra NJ, Koshiyama T, Yutani K, Kanamaru S, Arisaka F, Hikage T, Suzu. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-21

This repeat composes the C-terminal part of the bacteriophage T4 baseplate protein Gp5. This region of the protein forms a needle like projection from the baseplate that is presumed to puncture the bacterial cell membrane. Structurally three copies of the repeated region trimerise to form a beta solenoid type structure [1]. This family also includes repeats from bacterial Vgr proteins. [1]. 11823865. Structure of the cell-puncturing device of bacteriophage T4. Kanamaru S, Leiman PG, Kostyuchenko VA, Chipman PR, Mesyanzhinov VV, Arisaka F, Rossmann MG;. Nature 2002;415:553-557. (from Pfam)

Date:

2024-10-16

Family of bacterial and phage baseplate assembly proteins responsible for forming the small spike at the end of the tail or bacterial pathogenic needle-shaft [1]. This entry represents the OB fold part of the structure. This structure contains an unusual extra beta hairpin that forms the foundation of the spike protein's beta helix [3]. [1]. 7483254. Bacteriophage P2: genes involved in baseplate assembly. Haggard-Ljungquist E, Jacobsen E, Rishovd S, Six EW, Nilssen O, Sunshine MG, Lindqvist BH, Kim KJ, Barreiro V, Koonin EV, et al.;. Virology 1995;213:109-121. [2]. 24381728. The rise of the Type VI secretion system. Filloux A;. F1000Prime Rep. 2013;5:52. [3]. 22325780. Phage pierces the host cell membrane with the iron-loaded spike. Browning C, Shneider MM, Bowman VD, Schwarzer D, Leiman PG;. Structure. 2012;20:326-339. (from Pfam)

Date:

2024-10-16

VgrG proteins of bacterial type VI secretion systems (T6SS), Pvc8 of the Photorhabdus virulence cassette, and related proteins of phage baseplate assemblies, all members of this family, share the property of occurring at the tip of cell-puncturing contractile injection systems.

Date:

2024-10-16

VgrG (TssI in the revised nomenclature) is the spike protein at the tip of the apparatus of type VI secretion systems. Members of the VgrG family may have an attached effector domain. Effectors encoded as separate polypeptides are termed cargo effectors, while effectors encoded as a fusion with an apparatus component (VgrG, Hcp, or a PAAR protein) are called specialized.

Gene:

tssI

Date:

2024-08-07

This HMM represents the Vgr family of proteins, associated with some classes of Rhs elements. This model does not include a large octapeptide repeat region, VGXXXXXX, found in the Vgr of Rhs classes G and E.

Gene:

vgrG

Date:

2019-09-10

type VI secretion system Vgr family protein such as type VI secretion system tip protein VgrG, a core component and effector of Type VI secretion systems (T6SSs) that are involved in the pathogenicity of several Gram-negative bacteria

Date:

2024-05-09