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Conserved domains on  [gi|5726436|gb|AAD48437|]
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sortase [Staphylococcus aureus]

Protein Classification

sortase( domain architecture ID 10795668)

sortase is a cysteine transpeptidase that cleaves a substrate protein at a conserved cell wall sorting signal and covalently links it to peptidoglycan

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sortase_fam TIGR01076
LPXTG-site transpeptidase (sortase) family protein; This family includes Staphylococcus aureus ...
 74-206 4.41e-60

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: 184.23  E-value: 4.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436     74 GYIEIPDADIKEPVYPGPA--TPEQLNRGVSFAEENESLDDQNISIAGHTFIdRPNYQFTNLKAAKKGSMVYFKVGNETR 151
Cdd:TIGR01076   1 GYLEIPSIDIELPVYPGTAedTLEKGLGHLEGTSLPVGGENTRIVITGHRGL-PTATMFTNLDKLKKGDMLYLHVGNEVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5726436    152 KYKMTSIRDVKPTDVGVLDEQKGKDkQLTLITCDDYNEKT---GVWEKRKIFVATEVK 206
Cdd:TIGR01076  80 TYQVTSTKIVEPTDTEVLLIQHGKD-YLTLITCTPYMINThrlLVRGKRIPYVATEDE 136
 
Name Accession Description Interval E-value
sortase_fam TIGR01076
LPXTG-site transpeptidase (sortase) family protein; This family includes Staphylococcus aureus ...
 74-206 4.41e-60

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: 184.23  E-value: 4.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436     74 GYIEIPDADIKEPVYPGPA--TPEQLNRGVSFAEENESLDDQNISIAGHTFIdRPNYQFTNLKAAKKGSMVYFKVGNETR 151
Cdd:TIGR01076   1 GYLEIPSIDIELPVYPGTAedTLEKGLGHLEGTSLPVGGENTRIVITGHRGL-PTATMFTNLDKLKKGDMLYLHVGNEVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5726436    152 KYKMTSIRDVKPTDVGVLDEQKGKDkQLTLITCDDYNEKT---GVWEKRKIFVATEVK 206
Cdd:TIGR01076  80 TYQVTSTKIVEPTDTEVLLIQHGKD-YLTLITCTPYMINThrlLVRGKRIPYVATEDE 136
Sortase_A cd06165
Sortase domain found in class A sortases; Class A sortases are membrane-bound cysteine ...
 70-203 2.23e-32

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: 113.37  E-value: 2.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   70 SKVAGYIEIPDADIKEPVYPGpATPEQLNRGVSFAEENESLDDQNISIAGHTFIDrPNYQFTNLKAAKKGSMVYFKVGNE 149
Cdd:cd06165   1 LNVIGAIAIPSVGINLPIFKG-LSNENLLVGAGTMKPNQKMGKGNYVLAGHNMGD-GGLLFSPLQNLKKGDKIYLTDLKK 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 5726436  150 TRKYKMTSIRDVKPTDVGVLDEQKGKdKQLTLITCDDYNEktgvWEKRKIFVAT 203
Cdd:cd06165  79 VYEYKVTSKKVVDPTDVDVLDDTKGK-PLLTLITCDDPTD----TTKRIVVQGE 127
Sortase pfam04203
Sortase domain; The founder member of this family is S. aureus sortase, a transpeptidase that ...
 76-203 6.59e-26

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: 96.54  E-value: 6.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436     76 IEIPDADIKEPVYPGpATPEQLNRGVSFAEENESLDD-QNISIAGHTFIDrpNYQFTNLKAAKKGSMVYFKVGNETRKYK 154
Cdd:pfam04203   1 LEIPAIGVDAPVLEG-TSGEVLKYGVGHYDGTAMPGEkGNFVLAGHRMGG--GTVFARLDKLKKGDKIYVTTDGKTYTYR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 5726436    155 MTSIRDVKPTDVGVLDEQKGKDkQLTLITCDdynekTGVWEKRKIFVAT 203
Cdd:pfam04203  78 VTSVEVVDPDDVSVLDPTPGDP-ILTLITCT-----PPSYTKRLVVYAK 120
SrtA COG3764
Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis];
72-206 4.95e-25

Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442978  Cd Length: 144  Bit Score: 94.89  E-value: 4.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   72 VAGYIEIPDADIKEPVYPGpATPEQLNRGVSFAEENeSL--DDQNISIAGHTFIDRPNYqFTNLKAAKKGSMVYFKVGNE 149
Cdd:COG3764  13 LIGRLEIPKIGVDLPIVEG-TDEDTLAKGAGHYPGT-ALpgEVGNAVLAGHRDTPGGTV-FRRLDELKPGDEIYVETADG 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5726436  150 TRKYKMTSIRDVKPTDVGVLDeQKGKDkQLTLITCDDYNEKTgvweKRKIFVATEVK 206
Cdd:COG3764  90 TYTYRVTSIEVVDPDDVEVLA-PTGKP-LLTLITCTPFGSNT----DRLIVYAELVS 140
class_C_sortase NF033745
class C sortase;
13-187 5.79e-20

class C sortase;


Pssm-ID: 468165  Cd Length: 218  Bit Score: 83.69  E-value: 5.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436    13 GVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAK----------PQIP---------------- 66
Cdd:NF033745   1 LILLFLVGLGILLYPFVSNYYNNYQQSQAIAEYDKKVAKLSKEEIEKLLEkakayneelaGDGPvvdpftskdeeyaeye 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436    67 ----KDKSKVAGYIEIPDADIKEPVYPGpATPEQLNRGVSFAeENESL----DDQNISIAGHTFIdrPNYQ-FTNLKAAK 137
Cdd:NF033745  81 sqlnVNETGVMGYIEIPKINVKLPIYHG-TSEEVLQKGAGHL-EGTSLpvggKGTHSVITGHRGL--PSATlFTDLDKLK 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 5726436   138 KGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKqLTLITCDDY 187
Cdd:NF033745 157 KGDKFYIHVLGETLAYKVDQIKVVLPDDTDKLKIVPGKDL-VTLLTCTPY 205
 
Name Accession Description Interval E-value
sortase_fam TIGR01076
LPXTG-site transpeptidase (sortase) family protein; This family includes Staphylococcus aureus ...
 74-206 4.41e-60

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: 184.23  E-value: 4.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436     74 GYIEIPDADIKEPVYPGPA--TPEQLNRGVSFAEENESLDDQNISIAGHTFIdRPNYQFTNLKAAKKGSMVYFKVGNETR 151
Cdd:TIGR01076   1 GYLEIPSIDIELPVYPGTAedTLEKGLGHLEGTSLPVGGENTRIVITGHRGL-PTATMFTNLDKLKKGDMLYLHVGNEVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5726436    152 KYKMTSIRDVKPTDVGVLDEQKGKDkQLTLITCDDYNEKT---GVWEKRKIFVATEVK 206
Cdd:TIGR01076  80 TYQVTSTKIVEPTDTEVLLIQHGKD-YLTLITCTPYMINThrlLVRGKRIPYVATEDE 136
Sortase_A cd06165
Sortase domain found in class A sortases; Class A sortases are membrane-bound cysteine ...
 70-203 2.23e-32

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: 113.37  E-value: 2.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   70 SKVAGYIEIPDADIKEPVYPGpATPEQLNRGVSFAEENESLDDQNISIAGHTFIDrPNYQFTNLKAAKKGSMVYFKVGNE 149
Cdd:cd06165   1 LNVIGAIAIPSVGINLPIFKG-LSNENLLVGAGTMKPNQKMGKGNYVLAGHNMGD-GGLLFSPLQNLKKGDKIYLTDLKK 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 5726436  150 TRKYKMTSIRDVKPTDVGVLDEQKGKdKQLTLITCDDYNEktgvWEKRKIFVAT 203
Cdd:cd06165  79 VYEYKVTSKKVVDPTDVDVLDDTKGK-PLLTLITCDDPTD----TTKRIVVQGE 127
Sortase cd00004
Sortase domain; Sortases are cysteine transpeptidases, mainly found in Gram-positive bacteria, ...
 70-202 6.37e-29

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: 104.59  E-value: 6.37e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   70 SKVAGYIEIPDADIKEPVYPGPaTPEQLNRGVSFAEENESLDDQNISIAGHTFidRPNYQFTNLKAAKKGSMVYFKVGNE 149
Cdd:cd00004   1 YEYIGILEIPKINLKLPVLSGT-SYENLKIAPGRYYGSALGENGNIVIAGHNG--NGGSHFGNLKKLKKGDEIYLTDKGK 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 5726436  150 TRKYKMTSIRDVKPTDVGVLDEQKGkDKQLTLITCDDYNEKtgvweKRKIFVA 202
Cdd:cd00004  78 TYTYKVTEIEEVEPTDVEVILVTSG-DKDLTLITCTPYNGT-----KRLIVRA 124
Sortase pfam04203
Sortase domain; The founder member of this family is S. aureus sortase, a transpeptidase that ...
 76-203 6.59e-26

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: 96.54  E-value: 6.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436     76 IEIPDADIKEPVYPGpATPEQLNRGVSFAEENESLDD-QNISIAGHTFIDrpNYQFTNLKAAKKGSMVYFKVGNETRKYK 154
Cdd:pfam04203   1 LEIPAIGVDAPVLEG-TSGEVLKYGVGHYDGTAMPGEkGNFVLAGHRMGG--GTVFARLDKLKKGDKIYVTTDGKTYTYR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 5726436    155 MTSIRDVKPTDVGVLDEQKGKDkQLTLITCDdynekTGVWEKRKIFVAT 203
Cdd:pfam04203  78 VTSVEVVDPDDVSVLDPTPGDP-ILTLITCT-----PPSYTKRLVVYAK 120
SrtA COG3764
Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis];
72-206 4.95e-25

Sortase (surface protein transpeptidase) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442978  Cd Length: 144  Bit Score: 94.89  E-value: 4.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   72 VAGYIEIPDADIKEPVYPGpATPEQLNRGVSFAEENeSL--DDQNISIAGHTFIDRPNYqFTNLKAAKKGSMVYFKVGNE 149
Cdd:COG3764  13 LIGRLEIPKIGVDLPIVEG-TDEDTLAKGAGHYPGT-ALpgEVGNAVLAGHRDTPGGTV-FRRLDELKPGDEIYVETADG 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5726436  150 TRKYKMTSIRDVKPTDVGVLDeQKGKDkQLTLITCDDYNEKTgvweKRKIFVATEVK 206
Cdd:COG3764  90 TYTYRVTSIEVVDPDDVEVLA-PTGKP-LLTLITCTPFGSNT----DRLIVYAELVS 140
Sortase_D_2 cd06166
Sortase domain found in subfamily 2 of the class D family of sortases; Class D sortases are ...
 71-188 1.61e-24

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: 93.31  E-value: 1.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   71 KVAGYIEIPDADIKEPVYPGpATPEQLNRGVSFAEENESLDDQ-NISIAGH---TFidrpNYQFTNLKAAKKGSMVYFKV 146
Cdd:cd06166   2 GVIGILEIPKIDLKLPILEG-ATEENLKYGVGHFEGTAMPGEGgNFAIAGHrsyTY----GRFFNRLDELKIGDEIIVTT 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 5726436  147 GNETRKYKMTSIRDVKPTDVGVLDEQKGKdKQLTLITCDDYN 188
Cdd:cd06166  77 KNGTYTYKVTEIFIVEPTDVSVLDPTEGK-KEITLITCTPIN 117
Sortase_C cd05827
Sortase domain found in class C sortases; Class C sortases are membrane-bound cysteine ...
 70-187 5.19e-23

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: 89.38  E-value: 5.19e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   70 SKVAGYIEIPDADIKEPVYPGpATPEQLNRGVSFAEeNESL----DDQNISIAGHTfiDRPNYQ-FTNLKAAKKGSMVYF 144
Cdd:cd05827   1 DGVIGYLEIPKIDVDLPIYHG-TSEEVLAKGAGHLE-GTSLpvggKGTHSVIAGHR--GLPNATlFTDLDKLKKGDKFYI 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 5726436  145 KVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKqLTLITCDDY 187
Cdd:cd05827  77 TVLGETLAYKVDDIKVILPDDTDKLKIQPGKDL-VTLLTCTPY 118
class_C_sortase NF033745
class C sortase;
13-187 5.79e-20

class C sortase;


Pssm-ID: 468165  Cd Length: 218  Bit Score: 83.69  E-value: 5.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436    13 GVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAK----------PQIP---------------- 66
Cdd:NF033745   1 LILLFLVGLGILLYPFVSNYYNNYQQSQAIAEYDKKVAKLSKEEIEKLLEkakayneelaGDGPvvdpftskdeeyaeye 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436    67 ----KDKSKVAGYIEIPDADIKEPVYPGpATPEQLNRGVSFAeENESL----DDQNISIAGHTFIdrPNYQ-FTNLKAAK 137
Cdd:NF033745  81 sqlnVNETGVMGYIEIPKINVKLPIYHG-TSEEVLQKGAGHL-EGTSLpvggKGTHSVITGHRGL--PSATlFTDLDKLK 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 5726436   138 KGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKqLTLITCDDY 187
Cdd:NF033745 157 KGDKFYIHVLGETLAYKVDQIKVVLPDDTDKLKIVPGKDL-VTLLTCTPY 205
Sortase_D_1 cd05828
Sortase domain found in subfamily 1 of the class D family of sortases; Class D sortases are ...
 74-184 7.48e-15

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: 67.91  E-value: 7.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   74 GYIEIPDADIKEPVYPGpATPEQLNRGV----SFAEENESlddQNISIAGH--TFidrpnyqFTNLKAAKKGSMVYFKVG 147
Cdd:cd05828   5 ARLSIPRLGLDLPVLEG-TSGEALAFGPghlpGSALPGEG---GNVVIAGHrdTH-------FRFLKDLKVGDEITLETS 73

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 5726436  148 NETRKYKMTSIRDVKPTDVGVLDEQkgKDKQLTLITC 184
Cdd:cd05828  74 GGTYTYRVTETRIVDADDTSVLLPT--DEETLTLVTC 108
Sortase_E cd05830
Sortase domain found in the class E family of sortases; Class E sortases are membrane-bound ...
 74-185 1.14e-06

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: 46.05  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436   74 GYIEIP-DADIKEPVYPGpATPEQLNRGV------SFAEENeslddQNISIAGHtfidRPNY--QFTNLKAAKKGSMVYF 144
Cdd:cd05830   5 AVLYIPrFIDLDRPVVEG-TSEVLLRRGVghypgtALPGEV-----GNFAIAGH----RTTYgaPFRDLDELRPGDPIVV 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 5726436  145 KVGNETRKYKMTSIRDVKPTDVGVLDEQKGK------DKQLTLITCD 185
Cdd:cd05830  75 ETAGGWYVYRVTSTEIVSPDDVEVLAPVPGQpgappgRRLLTLTTCH 121
Sortase_F cd05829
Sortase domain found in the class F family of sortases; Class F sortases are mainly present in ...
 117-203 2.85e-05

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: 42.22  E-value: 2.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5726436  117 IAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGN-ETRKYKMTSIRDVKPTDVGVLDE-QKGKDKQLTLITCD-DYNEKTGV 193
Cdd:cd05829  55 IAGHVDSGGGPGVFARLGDLRPGDEVTVTRADgTTATFRVTSVETYPKDDLPTDEVfGPTGPPRLRLITCGgAFDRGTGS 134

                        90
                ....*....|
gi 5726436  194 WEKRKIFVAT 203
Cdd:cd05829 135 YEDNVVVYAE 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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