SrtB family sortase [Streptococcus sp. HMSC074F05]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| SrtB_LPKTxSAVK | NF040525 | class B sortase, LPKTxAVK-specific; This branch of the class B sortase family is found in ... |
30-279 | 0e+00 | |||||
class B sortase, LPKTxAVK-specific; This branch of the class B sortase family is found in multiple species of Streptococcus and Gemella. It processes target proteins that end with the motif LPKTxAVK-COOH, which differ from most sortase recognition sites in lacking an additional C-terminal transmembrane helix. Substrates of this sortase include the amylase-binding adhesin AbpA, as well of other proteins with similar N-terminal and C-terminal domains but unrelated central regions. : Pssm-ID: 439740 Cd Length: 261 Bit Score: 519.15 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| SrtB_LPKTxSAVK | NF040525 | class B sortase, LPKTxAVK-specific; This branch of the class B sortase family is found in ... |
30-279 | 0e+00 | |||||
class B sortase, LPKTxAVK-specific; This branch of the class B sortase family is found in multiple species of Streptococcus and Gemella. It processes target proteins that end with the motif LPKTxAVK-COOH, which differ from most sortase recognition sites in lacking an additional C-terminal transmembrane helix. Substrates of this sortase include the amylase-binding adhesin AbpA, as well of other proteins with similar N-terminal and C-terminal domains but unrelated central regions. Pssm-ID: 439740 Cd Length: 261 Bit Score: 519.15 E-value: 0e+00
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| sortase_srtB | TIGR03064 | sortase, SrtB family; Members of this transpeptidase family are, in most cases, designated ... |
50-252 | 2.62e-69 | |||||
sortase, SrtB family; Members of this transpeptidase family are, in most cases, designated sortase B, product of the srtB gene. This protein shows only distant similarity to the sortase A family, for which there may be several members in a single bacterial genome. Typical SrtB substrate motifs include NAKTN, NPKSS, etc, and otherwise resemble the LPXTG sorting signals recognized by sortase A proteins. [Cell envelope, Other, Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 211782 Cd Length: 232 Bit Score: 214.13 E-value: 2.62e-69
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| COG4509 | COG4509 | Uncharacterized conserved protein [Function unknown]; |
56-259 | 2.53e-62 | |||||
Uncharacterized conserved protein [Function unknown]; Pssm-ID: 443589 Cd Length: 245 Bit Score: 196.69 E-value: 2.53e-62
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| Sortase_B | cd05826 | Sortase domain found in class B sortases; Class B sortases are membrane-bound cysteine ... |
81-249 | 2.81e-51 | |||||
Sortase domain found in class B sortases; Class B sortases are membrane-bound cysteine transpeptidases broadly distributed in Gram-positive bacteria (mainly present in Firmicutes and Actinobacteria). They can have radically distinct functions. Some members of this group attach haemoproteins to the peptidoglycan of the cell wall, while others assemble pili, which are multi-subunit hair-like fibres that extend from the cell surface to promote microbial adhesion and biofilm formation. In transpeptidation reaction, the surface protein substrate is cleaved at a conserved cell wall-sorting signal (Class B sortases normally recognize the consensus NP[Q/K][T/S][N/G/S][D/A] motif), and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical sortase B protein from Staphylococcus aureus (named Sa-SrtB) cleaves surface protein precursors between threonine and asparagine at a conserved NPQTN motif with subsequent covalent linkage to pentaglycine cross-bridges. It is required for anchoring the heme-iron binding surface protein IsdC to the cell wall envelope. SrtB contains an N-terminal hydrophobic region that functions as a signal peptide/transmembrane domain. At the C terminus, it contains an essential cysteine residue within the catalytic TLXTC signature sequence, where X is usually a serine. Genes encoding SrtB and its targets are generally clustered in the same locus. The prototypical class B sortase involved in pilus biogenesis is pilus-specific sortase C2 from Streptococcus pyogenes (named Sp-SrtC2) that anchors a surface protein containing a QVPTGV motif to the cell wall, as well as polymerizes the major pilin subunit Tee3/FctA and attaches the minor tip pilin Cpa. The linkage of Cpa to Tee3 by SrtC2 requires the VPPTG motif in the cell wall-sorting signal of Cpa. The family also includes SrtB enzymes from Bacillus anthracis (named Ba-SrtB) and Clostridium difficile (named Cd-SrtB). Ba-SrtB is thought to recognize the NPKTG motif, and attaches surface proteins to meso-diaminopimelic acid (mDAP) cross-bridges. Cd-SrtB does not play an essential role in pathogenesis. It cleaves short [SP]PXTG motif-containing peptides between the threonine and glycine residues and then covalently anchors the threonine residue to a nucleophile such as glycine or mDAP, but not to the peptidoglycan of C. difficile, suggesting a novel association of sortase activity with cyclic diGMP (c-diGMP)-mediated regulation to control levels of cell wall anchoring and secretion of putative adhesion molecules. Pssm-ID: 320675 Cd Length: 170 Bit Score: 165.72 E-value: 2.81e-51
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| Name | Accession | Description | Interval | E-value | |||||
| SrtB_LPKTxSAVK | NF040525 | class B sortase, LPKTxAVK-specific; This branch of the class B sortase family is found in ... |
30-279 | 0e+00 | |||||
class B sortase, LPKTxAVK-specific; This branch of the class B sortase family is found in multiple species of Streptococcus and Gemella. It processes target proteins that end with the motif LPKTxAVK-COOH, which differ from most sortase recognition sites in lacking an additional C-terminal transmembrane helix. Substrates of this sortase include the amylase-binding adhesin AbpA, as well of other proteins with similar N-terminal and C-terminal domains but unrelated central regions. Pssm-ID: 439740 Cd Length: 261 Bit Score: 519.15 E-value: 0e+00
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| sortase_srtB | TIGR03064 | sortase, SrtB family; Members of this transpeptidase family are, in most cases, designated ... |
50-252 | 2.62e-69 | |||||
sortase, SrtB family; Members of this transpeptidase family are, in most cases, designated sortase B, product of the srtB gene. This protein shows only distant similarity to the sortase A family, for which there may be several members in a single bacterial genome. Typical SrtB substrate motifs include NAKTN, NPKSS, etc, and otherwise resemble the LPXTG sorting signals recognized by sortase A proteins. [Cell envelope, Other, Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 211782 Cd Length: 232 Bit Score: 214.13 E-value: 2.62e-69
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| COG4509 | COG4509 | Uncharacterized conserved protein [Function unknown]; |
56-259 | 2.53e-62 | |||||
Uncharacterized conserved protein [Function unknown]; Pssm-ID: 443589 Cd Length: 245 Bit Score: 196.69 E-value: 2.53e-62
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| Sortase_B | cd05826 | Sortase domain found in class B sortases; Class B sortases are membrane-bound cysteine ... |
81-249 | 2.81e-51 | |||||
Sortase domain found in class B sortases; Class B sortases are membrane-bound cysteine transpeptidases broadly distributed in Gram-positive bacteria (mainly present in Firmicutes and Actinobacteria). They can have radically distinct functions. Some members of this group attach haemoproteins to the peptidoglycan of the cell wall, while others assemble pili, which are multi-subunit hair-like fibres that extend from the cell surface to promote microbial adhesion and biofilm formation. In transpeptidation reaction, the surface protein substrate is cleaved at a conserved cell wall-sorting signal (Class B sortases normally recognize the consensus NP[Q/K][T/S][N/G/S][D/A] motif), and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical sortase B protein from Staphylococcus aureus (named Sa-SrtB) cleaves surface protein precursors between threonine and asparagine at a conserved NPQTN motif with subsequent covalent linkage to pentaglycine cross-bridges. It is required for anchoring the heme-iron binding surface protein IsdC to the cell wall envelope. SrtB contains an N-terminal hydrophobic region that functions as a signal peptide/transmembrane domain. At the C terminus, it contains an essential cysteine residue within the catalytic TLXTC signature sequence, where X is usually a serine. Genes encoding SrtB and its targets are generally clustered in the same locus. The prototypical class B sortase involved in pilus biogenesis is pilus-specific sortase C2 from Streptococcus pyogenes (named Sp-SrtC2) that anchors a surface protein containing a QVPTGV motif to the cell wall, as well as polymerizes the major pilin subunit Tee3/FctA and attaches the minor tip pilin Cpa. The linkage of Cpa to Tee3 by SrtC2 requires the VPPTG motif in the cell wall-sorting signal of Cpa. The family also includes SrtB enzymes from Bacillus anthracis (named Ba-SrtB) and Clostridium difficile (named Cd-SrtB). Ba-SrtB is thought to recognize the NPKTG motif, and attaches surface proteins to meso-diaminopimelic acid (mDAP) cross-bridges. Cd-SrtB does not play an essential role in pathogenesis. It cleaves short [SP]PXTG motif-containing peptides between the threonine and glycine residues and then covalently anchors the threonine residue to a nucleophile such as glycine or mDAP, but not to the peptidoglycan of C. difficile, suggesting a novel association of sortase activity with cyclic diGMP (c-diGMP)-mediated regulation to control levels of cell wall anchoring and secretion of putative adhesion molecules. Pssm-ID: 320675 Cd Length: 170 Bit Score: 165.72 E-value: 2.81e-51
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