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GspD-like, N0 domain
GspD is a type II general secretion pathway protein involved in protein export. This is the N0 domain found at the N-terminal of GspD type II secretins and its close homologues [1-5]. These proteins form a dodecameric ring, in which the N0 domain mediate extensive contacts suggesting that dodecameric N0 ring is an important feature of T2SS secretins [4]. This domain is also found in virion export proteins, proteins thought to form a channel across the host outer membrane for the purposes of extruding the bacteriophage. Paper describing PDB structure 3ezj. [1]. 19217396. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Korotkov KV, Pardon E, Steyaert J, Hol WG;. Structure. 2009;17:255-265. Paper describing PDB structure 3oss. [2]. 21931548. Structural and functional studies on the interaction of GspC and GspD in the type II secretion system. Korotkov KV, Johnson TL, Jobling MG, Pruneda J, Pardon E, Heroux A, Turley S, Steyaert J, Holmes RK, Sandkvist M, Hol WG;. PLoS Pathog. 2011;7:e1002228. Paper describing PDB structure 4e9j. [3]. 23188826. New insights into the assembly of bacterial secretins: structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa. Van der Meeren R, Wen Y, Van Gelder P, Tommassen J, Devreese B, Savvides SN;. J Biol Chem. 2013;288:1214-1225. Paper describing PDB structure 4jtm. [4]. 23820381. A dodecameric ring-like structure of the N0 domain of the type II secretin from enterotoxigenic Escherichia coli. Korotkov KV, Delarosa JR, Hol WGJ;. J Struct Biol. 2013;183:354-362. Paper describing PDB structure 5mp2. . TRUNCATED at 1650 bytes (from Pfam)
AMIN domain-containing protein
This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localises to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localisation of periplasmic protein complexes [1]. [1]. 18723522. AMIN domains have a predicted role in localization of diverse periplasmic protein complexes. de Souza RF, Anantharaman V, de Souza SJ, Aravind L, Gueiros-Filho FJ;. Bioinformatics. 2008;24:2423-2426. (from Pfam)
secretin N-terminal domain-containing protein
This is a short, often repeated, domain found in bacterial type II/III secretory system proteins. All previous NolW-like domains fall into this family. (from Pfam)
type IV pilus secretin family protein
type IV pilus secretin family protein such as PilQ, which is required for type IV pilus biogenesis and competence, and could function as a pore for exit of the pilus but also as a channel for entry of heme and antimicrobial agents and uptake of transforming DNA
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