srtA

Sortase A

222 amino acids

Transpeptidase that anchors surface proteins to the cell wall (PubMed:11854224, PubMed:11929538, PubMed:16247833, PubMed:22837151). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:11929538). Involved in pathogenesis (PubMed:11854224, PubMed:11929538, PubMed:15028680). May regulate the rate of synthesis and/or the stability of a subset of LPXTG proteins (PubMed:22837151). Not involved in cell wall-anchoring of Hbp2 (SvpA) or Hbp1 (PubMed:15028680, PubMed:16247833).

Belongs to the bacterial sortase family. Class A subfamily.

24.712 kDa

MLKKTIAIIILIIGLLLIFSPFIKNGIVKYMSGHETIEQYKASDIKKNNEKDATFDFESVQLPSMTSVIKGAANYDKDAVVGSIAVPSVDVNLLVFKGTNTANLLAGATTMRSDQVMGKGNYPLAGHHMRDESMLFGPIMKVKKGDKIYLTDLENLYEYTVTETKTIDETEVSVIDNTKDARITLITCDKPTETTKRFVAVGELEKTEKLTKELENKYFPSK

srtA

Sortase A

210 amino acids

Transpeptidase that anchors surface proteins to the cell wall (PubMed:15968076). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (PubMed:15968076). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:15968076). Important for growth in macrophages. May be critical in the early stages of inhalation anthrax (PubMed:16041044).

Belongs to the bacterial sortase family. Class A subfamily.

23.151 kDa

MNKQRIYSIVAILLFVVGGVLIGKPFYDGYQAEKKQTENVQAVQKMDYEKHETEFVDASKIDQPDLAEVANASLDKKQVIGRISIPSVSLELPVLKSSTEKNLLSGAATVKENQVMGKGNYALAGHNMSKKGVLFSDIASLKKGDKIYLYDNENEYEYAVTGVSEVTPDKWEVVEDHGKDEITLITCVSVKDNSKRYVVAGDLVGTKAKK

srtA

Sortase A

206 amino acids

Transpeptidase that anchors surface proteins to the cell wall (PubMed:10427003, PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Utilizes lipid II as the peptidoglycan substrate for the sorting reaction (PubMed:10446208, PubMed:11856734). Responsible for the display of important virulence factors (PubMed:14769030). Important for interactions with the host and host colonization during infection (PubMed:10805806, PubMed:14769030).

Belongs to the bacterial sortase family. Class A subfamily.

23.541 kDa

MKKWTNRLMTIAGVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKDKSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK

srtA

Lantibiotic streptin

46 amino acids

Lanthionine-containing peptide antibiotic (lantibiotic) active on certain Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores (By similarity).

Belongs to the type A lantibiotic family.

5.219 kDa

MNNTIKDFDLDLKTNKKDTATPYVGSRYLCTPGSCWKLVCFTTTVK

srtA

Lantibiotic streptin

46 amino acids

Lanthionine-containing peptide antibiotic (lantibiotic) active on certain Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.

Belongs to the type A lantibiotic family.

5.219 kDa

MNNTIKDFDLDLKTNKKDTATPYVGSRYLCTPGSCWKLVCFTTTVK