MULTISPECIES: class A sortase [Enterococcus]
Protein Classification
class A sortase( domain architecture ID 10150464)
class A sortase is a cysteine transpeptidase that cleaves a substrate protein at a conserved cell wall sorting signal and covalently links it to peptidoglycan and performs a housekeeping role
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| Sortase_A | cd06165 | Sortase domain found in class A sortases; Class A sortases are membrane-bound cysteine ... |
89-214 | 9.27e-67 | |||
Sortase domain found in class A sortases; Class A sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). They perform a housekeeping role in the cell as members of this group are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They do so by catalyzing a transpeptidation reaction in which the surface protein substrate is cleaved at a conserved cell wall-sorting signal (Class A sortases recognize a canonical LPXTG motif, X can be any amino acid), and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical sortase A protein from Staphylococcus aureus (named Sa-SrtA) cleaves the amide bond between threonine and glycine residues of the canonical LPXTG motif in a wide range of protein substrates with diverse functions that can promote bacterial adhesion, nutrient acquisition, host cell invasion, and immune evasion. Next, it catalyzes a transpeptidation reaction by which the proteins are covalently linked to the peptidoglycan precursor lipid II. SrtA is therefore affects the ability of a pathogen to establish successful infection. SrtA contains an N-terminal hydrophobic segment, a linker region and an extra-cellular C-terminal catalytic domain. The hydrophobic segment functions as both a signal peptide for secretion and a stop-transfer signal for membrane anchoring. The catalytic domain contains the catalytic TLXTC signature sequence where X is usually a valine, isoleucine or a threonine. The gene encoding SrtA is generally not located in the same gene cluster as its substrates while the gene encoding SrtB is usually clustered in the same locus as its substrate. : Pssm-ID: 320680 Cd Length: 127 Bit Score: 202.35 E-value: 9.27e-67
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| Name | Accession | Description | Interval | E-value | ||||
| Sortase_A | cd06165 | Sortase domain found in class A sortases; Class A sortases are membrane-bound cysteine ... |
89-214 | 9.27e-67 | ||||
Sortase domain found in class A sortases; Class A sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). They perform a housekeeping role in the cell as members of this group are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They do so by catalyzing a transpeptidation reaction in which the surface protein substrate is cleaved at a conserved cell wall-sorting signal (Class A sortases recognize a canonical LPXTG motif, X can be any amino acid), and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical sortase A protein from Staphylococcus aureus (named Sa-SrtA) cleaves the amide bond between threonine and glycine residues of the canonical LPXTG motif in a wide range of protein substrates with diverse functions that can promote bacterial adhesion, nutrient acquisition, host cell invasion, and immune evasion. Next, it catalyzes a transpeptidation reaction by which the proteins are covalently linked to the peptidoglycan precursor lipid II. SrtA is therefore affects the ability of a pathogen to establish successful infection. SrtA contains an N-terminal hydrophobic segment, a linker region and an extra-cellular C-terminal catalytic domain. The hydrophobic segment functions as both a signal peptide for secretion and a stop-transfer signal for membrane anchoring. The catalytic domain contains the catalytic TLXTC signature sequence where X is usually a valine, isoleucine or a threonine. The gene encoding SrtA is generally not located in the same gene cluster as its substrates while the gene encoding SrtB is usually clustered in the same locus as its substrate. Pssm-ID: 320680 Cd Length: 127 Bit Score: 202.35 E-value: 9.27e-67
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| SrtA | COG3764 | Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis]; |
91-220 | 4.02e-37 | ||||
Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442978 Cd Length: 144 Bit Score: 127.25 E-value: 4.02e-37
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| Sortase | pfam04203 | Sortase domain; The founder member of this family is S. aureus sortase, a transpeptidase that ... |
95-215 | 2.36e-32 | ||||
Sortase domain; The founder member of this family is S. aureus sortase, a transpeptidase that attaches surface proteins by the threonine of an LPXTG motif to the cell wall. Pssm-ID: 427781 Cd Length: 121 Bit Score: 114.26 E-value: 2.36e-32
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| class_C_sortase | NF033745 | class C sortase; |
18-200 | 1.05e-23 | ||||
class C sortase; Pssm-ID: 468165 Cd Length: 218 Bit Score: 94.86 E-value: 1.05e-23
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| sortase_fam | TIGR01076 | LPXTG-site transpeptidase (sortase) family protein; This family includes Staphylococcus aureus ... |
93-223 | 2.27e-18 | ||||
LPXTG-site transpeptidase (sortase) family protein; This family includes Staphylococcus aureus sortase, a transpeptidase that attaches surface proteins by the Thr of an LPXTG motif to the cell wall. It also includes a protein required for correct assembly of an LPXTG-containing fimbrial protein, a set of homologous proteins from Streptococcus pneumoniae, in which LPXTG proteins are common. However, related proteins are found in Bacillus subtilis and Methanobacterium thermoautotrophicum, in which LPXTG-mediated cell wall attachment is not known. [Cell envelope, Other, Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 130148 Cd Length: 136 Bit Score: 78.68 E-value: 2.27e-18
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| Name | Accession | Description | Interval | E-value | ||||
| Sortase_A | cd06165 | Sortase domain found in class A sortases; Class A sortases are membrane-bound cysteine ... |
89-214 | 9.27e-67 | ||||
Sortase domain found in class A sortases; Class A sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). They perform a housekeeping role in the cell as members of this group are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They do so by catalyzing a transpeptidation reaction in which the surface protein substrate is cleaved at a conserved cell wall-sorting signal (Class A sortases recognize a canonical LPXTG motif, X can be any amino acid), and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical sortase A protein from Staphylococcus aureus (named Sa-SrtA) cleaves the amide bond between threonine and glycine residues of the canonical LPXTG motif in a wide range of protein substrates with diverse functions that can promote bacterial adhesion, nutrient acquisition, host cell invasion, and immune evasion. Next, it catalyzes a transpeptidation reaction by which the proteins are covalently linked to the peptidoglycan precursor lipid II. SrtA is therefore affects the ability of a pathogen to establish successful infection. SrtA contains an N-terminal hydrophobic segment, a linker region and an extra-cellular C-terminal catalytic domain. The hydrophobic segment functions as both a signal peptide for secretion and a stop-transfer signal for membrane anchoring. The catalytic domain contains the catalytic TLXTC signature sequence where X is usually a valine, isoleucine or a threonine. The gene encoding SrtA is generally not located in the same gene cluster as its substrates while the gene encoding SrtB is usually clustered in the same locus as its substrate. Pssm-ID: 320680 Cd Length: 127 Bit Score: 202.35 E-value: 9.27e-67
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| SrtA | COG3764 | Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis]; |
91-220 | 4.02e-37 | ||||
Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442978 Cd Length: 144 Bit Score: 127.25 E-value: 4.02e-37
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| Sortase | cd00004 | Sortase domain; Sortases are cysteine transpeptidases, mainly found in Gram-positive bacteria, ... |
90-213 | 1.12e-33 | ||||
Sortase domain; Sortases are cysteine transpeptidases, mainly found in Gram-positive bacteria, which either anchor surface proteins to peptidoglycans of the bacterial cell wall envelope or link proteins together to form pili by working alone, or in concert with other enzymes. They do so by catalyzing a transpeptidation reaction in which the surface protein substrate is cleaved at a conserved cell wall sorting signal and covalently linked to peptidoglycan for display on the bacterial surface. Sortases are grouped into different classes based on sequence, membrane topology, genomic positioning, and cleavage site preference. The different classes are called class A to F sortases. Most Gram-positive bacteria contain more than one sortase and it is thought that the different sortases attach different surface protein classes. The typical eight-stranded beta-barrel fold is observed in all known sortases, along with the conserved catalytic triad consisting of cysteine, histidine and arginine residues. Some sortases contain an N-terminal signal peptide only and the C-terminus serves as a membrane anchor, which represents a type I membrane topology, with the N-terminal enzymatic portion projecting towards the bacterial surface and the C-terminal end residing in the cytoplasm. Other sortases adopt a type II membrane topology, with the N-terminal hydrophobic segment inside the cytoplasm and the C-terminal enzymatic portion located across the plasma membrane. The N-terminus either functions as both a signal peptide for secretion and a stop-transfer signal for membrane anchoring. Sortases are also present in some Gram-negative and Archaebacterial species, but the functions of these enzymes are unknown. Pssm-ID: 320674 Cd Length: 125 Bit Score: 118.07 E-value: 1.12e-33
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| Sortase | pfam04203 | Sortase domain; The founder member of this family is S. aureus sortase, a transpeptidase that ... |
95-215 | 2.36e-32 | ||||
Sortase domain; The founder member of this family is S. aureus sortase, a transpeptidase that attaches surface proteins by the threonine of an LPXTG motif to the cell wall. Pssm-ID: 427781 Cd Length: 121 Bit Score: 114.26 E-value: 2.36e-32
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| Sortase_D_2 | cd06166 | Sortase domain found in subfamily 2 of the class D family of sortases; Class D sortases are ... |
91-213 | 1.03e-31 | ||||
Sortase domain found in subfamily 2 of the class D family of sortases; Class D sortases are cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). They anchor surface proteins bearing a cell wall sorting signal to peptidoglycans of the bacterial cell wall envelope, which is responsible for spore formation under anaerobic conditions. This involves a transpeptidation reaction in which the surface protein substrate is cleaved at the cell wall sorting signal and covalently linked to peptidoglycan for display on the bacterial surface. The prototypical subfamily 2 of class D sortase from Clostridium perfringens (named Cp-SrtD) recognizes the LPQTGS signal motif for transpeptidation. Its catalytic activity is in a metal cation- and temperature- dependent manner. The presence of magnesium appears to enhance Cp-SrtD catalysis towards the LPQTGS signal motif. Pssm-ID: 320681 Cd Length: 127 Bit Score: 112.96 E-value: 1.03e-31
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| Sortase_C | cd05827 | Sortase domain found in class C sortases; Class C sortases are membrane-bound cysteine ... |
91-200 | 6.45e-26 | ||||
Sortase domain found in class C sortases; Class C sortases are membrane-bound cysteine transpeptidases broadly distributed in Gram-positive bacteria (mainly present in Firmicutes and Actinobacteria). They function as pilin polymerases responsible for the assembly of pili, which are multi-subunit hair-like fibres that extend from the cell surface to promote microbial adhesion and biofilm formation. First, one or more class C sortases form the long thin shaft of the pilus through linking together pilin subunits via isopeptide bonds. The base of the pilus is then anchored to the cell wall by a housekeeping sortase or, in some cases, the class C sortase itself. Depending upon the organism both the number and type of sortase enzymes involved varies, and in some cases, accessory factors appear to be needed. In three-component spaA pilus from Corynebacterium diphtheriae, the prototypical class C sortase (named Cd-SrtA) catalyzes polymerization of the SpaA-type pilus, consisting of the shaft pilin SpaA, tip pilin SpaC and minor pilin SpaB. The pilus shaft is then attached to the cell wall by a housekeeping class E sortase, Cd-SrtF. In the absence of Cd-SrtF, Cd-SrtA attaches the pilus to the cell wall, albeit at a reduced rate. Cd-SrtA can recognize two distinct sorting signals (LPLTG in SpaA and SpaC, and LAFTG in SpaB) and it can employ lysine residues that originate from different proteins (either Lys190 within the pilin motif of SpaA or Lys139 in SpaB). However, Cd-SrtA cannot be able to polymerize the major pilin subunit SpaH, even though it contains LPLTG motif. In two-component pili of prototypical Bacillus cereus, the class C sortase (named Bc-SrtD) cleaves related sorting signals within a major pilin protein BcpA (LPVTG) and a minor tip pilin BcpB (IPNTG), and catalyzes a transpeptidation that joins the threonine residues in each signal to the side-chain of Lys162 in BcpA (located within a pilin motif). Unlike the SpaA pilus in C. diphtheriae, in B. cereus Bc-SrtD is unable to covalently attach the pilus to the cell wall without the help of the housekeeping sortase. Pssm-ID: 320676 Cd Length: 131 Bit Score: 97.85 E-value: 6.45e-26
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| class_C_sortase | NF033745 | class C sortase; |
18-200 | 1.05e-23 | ||||
class C sortase; Pssm-ID: 468165 Cd Length: 218 Bit Score: 94.86 E-value: 1.05e-23
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| sortase_fam | TIGR01076 | LPXTG-site transpeptidase (sortase) family protein; This family includes Staphylococcus aureus ... |
93-223 | 2.27e-18 | ||||
LPXTG-site transpeptidase (sortase) family protein; This family includes Staphylococcus aureus sortase, a transpeptidase that attaches surface proteins by the Thr of an LPXTG motif to the cell wall. It also includes a protein required for correct assembly of an LPXTG-containing fimbrial protein, a set of homologous proteins from Streptococcus pneumoniae, in which LPXTG proteins are common. However, related proteins are found in Bacillus subtilis and Methanobacterium thermoautotrophicum, in which LPXTG-mediated cell wall attachment is not known. [Cell envelope, Other, Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 130148 Cd Length: 136 Bit Score: 78.68 E-value: 2.27e-18
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| Sortase_D_1 | cd05828 | Sortase domain found in subfamily 1 of the class D family of sortases; Class D sortases are ... |
91-200 | 2.15e-13 | ||||
Sortase domain found in subfamily 1 of the class D family of sortases; Class D sortases are cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Firmicutes). The prototypical subfamily 1 of class D sortase from Bacillus anthracis (named Ba-SrtC) covalently attaches proteins bearing a noncanonical LPNTA sorting signal, such as the BasH and BasI proteins, to the peptidoglycan of the cell wall that facilitate sporulation. BasH is exclusively anchored to the forespore cell wall envelope, while BasI is attached to the diaminopimelic acid moiety of the peptidoglycan of predivisional cells. Ba-SrtC lacks the N-terminal signal peptide and membrane anchor. The family also includes many class D sortase homologs from Gram-negative bacteria, but the functions of these enzymes are unknown. Pssm-ID: 320677 Cd Length: 127 Bit Score: 64.82 E-value: 2.15e-13
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| Sortase_E | cd05830 | Sortase domain found in the class E family of sortases; Class E sortases are membrane-bound ... |
90-214 | 2.81e-13 | ||||
Sortase domain found in the class E family of sortases; Class E sortases are membrane-bound cysteine transpeptidases distributed in Gram-positive bacteria (mainly present in Actinobacteria). Genes encoding class A and E sortases are never found in the same organism, and similar to class A sortases, the genes encoding class E sortases are not positioned adjacent to genes encoding potential protein substrates, suggesting a housekeeping sortase function of class E sortases in some high G + C Gram-positive bacteria. Similar to class A sortase, class E sortases are capable of anchoring a large number of functionally distinct surface proteins containing a cell wall sorting signal to an amino group located on the bacterial cell wall. They recognize an LAXTG sorting signal, instead of the canonical LPXTG motif processed by class A sortases. The prototypical class E sortase from Corynebacterium diphtheria (named Cd-SrtF) is a non-polymerization sortase that is not required for pilus polymerization, and proceeds to complete the assembly process by anchoring the polymer to the cell wall peptidoglycan. Moreover, in Streptomyces coelicolor, one or both of Staphylococcus aureus SrtA homologs may function as class E sortase responsible for the cell wall anchoring of the long chaplin proteins (ChpA-C) containing an LAXTG sorting signal, which presumably mediate aerial hyphae formation. The family also includes some class E sortase homologs from Gram-negative and Archaebacterial species, but the functions of these enzymes are unknown. Pssm-ID: 320679 Cd Length: 135 Bit Score: 64.92 E-value: 2.81e-13
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| Sortase_F | cd05829 | Sortase domain found in the class F family of sortases; Class F sortases are mainly present in ... |
135-202 | 1.62e-04 | ||||
Sortase domain found in the class F family of sortases; Class F sortases are mainly present in Actinobacteria, Chlorobacteria and Firmicutes. Their functions are largely unknown. Pssm-ID: 320678 Cd Length: 144 Bit Score: 40.68 E-value: 1.62e-04
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| Sortase_B | cd05826 | Sortase domain found in class B sortases; Class B sortases are membrane-bound cysteine ... |
138-215 | 3.97e-04 | ||||
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: 39.76 E-value: 3.97e-04
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