SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
13-453
1.82e-23
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
The actual alignment was detected with superfamily member NF033902:
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 103.68 E-value: 1.82e-23
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
13-453
1.82e-23
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 103.68 E-value: 1.82e-23
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.
Pssm-ID: 275067 [Multi-domain] Cd Length: 124 Bit Score: 76.15 E-value: 1.05e-16
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
356-417
1.33e-11
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 59.91 E-value: 1.33e-11
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
13-453
1.82e-23
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 103.68 E-value: 1.82e-23
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.
Pssm-ID: 275067 [Multi-domain] Cd Length: 124 Bit Score: 76.15 E-value: 1.05e-16
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
356-417
1.33e-11
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 59.91 E-value: 1.33e-11
Gram-positive pilin subunit D1, N-terminal domain; GramPos_pilinD1 is the first subunit domain ...
13-172
3.06e-05
Gram-positive pilin subunit D1, N-terminal domain; GramPos_pilinD1 is the first subunit domain of Gram-positive pilins from Strep.pneumoniae. There are three major pilin subunits that form the polymeric backbone of the pilin from S. pneumoniae, constructed of three Ig-like, CnaB, domains along with a crucial N-terminal domain, D1. The three IG-like domains are stabilized by internal Lys-Asn isopeptide bonds, but this N-terminal domain makes few contact with the rest of the molecule due to the different orientation of its G beta-strand. Strand G of D1 also carries the YPKN motif that provides the essential Lys residue for the sortase-mediated intermolecular linkages along the pilus shaft. Gram-positive pili are formed from a single chain of covalently linked subunit proteins (pilins), usually comprising an adhesin at the distal tip, a major pilin that forms the polymer shaft and a minor pilin that mediates cell wall anchoring at the base.
Pssm-ID: 465172 Cd Length: 161 Bit Score: 44.33 E-value: 3.06e-05
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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