sspB

Staphopain B

393 amino acids

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.

Belongs to the peptidase C47 family.

44.59 kDa

MNSSCKTRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLANNIKEKESAKTVSPQLKQELKTTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCATFPNQMIEYGKSQGRDIHYQEGVPSYNQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVANAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY

sspB

Staphopain B

393 amino acids

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.

Belongs to the peptidase C47 family.

44.611 kDa

MNSSYKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSSKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCSTFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY

sspB

Staphopain B

393 amino acids

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner (PubMed:20375568, PubMed:19284294). Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils (PubMed:19284294). Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin (PubMed:28438975).

Belongs to the peptidase C47 family.

44.576 kDa

MNSSCKTRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLANNIKEKESAKTVSPQLKQELKTTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCATFPNQMIEYGKSQGRDIHYQEGVPSYNQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY

sspB

Staphopain B

393 amino acids

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.

Belongs to the peptidase C47 family.

44.611 kDa

MNSSYKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSSKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCSTFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY

sspB

Staphopain B

393 amino acids

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.

Belongs to the peptidase C47 family.

44.519 kDa

MNSSCKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSAKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCATFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY

sspB

Staphopain B

393 amino acids

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.

Belongs to the peptidase C47 family.

44.519 kDa

MNSSCKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSAKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCATFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY

sspB

Staphopain B

393 amino acids

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.

Belongs to the peptidase C47 family.

44.595 kDa

MNSSYKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSAKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCSTFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY

sspB

Staphopain B

393 amino acids

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.

Belongs to the peptidase C47 family.

44.595 kDa

MNSSYKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSAKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCSTFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY

sspB

Stringent starvation protein B

165 amino acids

Seems to act in concert with SspA in the regulation of several proteins during exponential and stationary-phase growth. The exact function of SspB is not yet known (By similarity).

Belongs to the SspB family.

18.262 kDa

MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK

sspB

Stringent starvation protein B

165 amino acids

Also stimulates degradation of the N-terminus of RseA (residues 1-108, alone or in complex with sigma-E) by ClpX-ClpP in a non-ssrA-mediated fashion.

Belongs to the SspB family.

18.262 kDa

MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK

sspB

Stringent starvation protein B

165 amino acids

Also stimulates degradation of the N-terminus of RseA (residues 1-108, alone or in complex with sigma-E) by ClpX-ClpP in a non-ssrA-mediated fashion.

Belongs to the SspB family.

18.238 kDa

MDLSQLTPRRPYLLRAFYEWLLDNQLTPLLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK

sspB

Stringent starvation protein B homolog

150 amino acids

Also stimulates degradation of the N-terminus of RseA (residues 1-108, alone or in complex with sigma-E) by ClpX-ClpP in a non-ssrA-mediated fashion.

Belongs to the SspB family.

17.168 kDa

MEYKSSPKRPYLLRAYYDWLVDNSFTPYLVVDATYLGVNVPVEYVKDGQIVLNLSASATGNLQLTNDFIQFNARFKGVSRELYIPMGAALAIYARENGDGVMFEPEEIYDELNIEPDTEQPTGFYEAVDKPKKREEKKKTKSVSHLRIVD

sspB

Small, acid-soluble spore protein B

67 amino acids

SASP are bound to spore DNA. They are double-stranded DNA-binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light.

Belongs to the alpha/beta-type SASP family.

6.98 kDa

MANQNSSNDLLVPGAAQAIDQMKLEIASEFGVNLGADTTSRANGSVGGEITKRLVSFAQQQMGGRVQ