sspA

Glutamyl endopeptidase

357 amino acids

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).

Belongs to the peptidase S1B family.

38.639 kDa

MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQTDKQQTPKIQKGGNLKPLEQRERANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHIVDATHGDPHALKAFASAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNQFNGAVFINENVRNFLKQNIEDINFANDDHPNNPDNPDNPNNPDNPNNPDNPNNPDNPDNPNNPDNPNNPDNPNNPDQPNNPNNPDNGDNNNSDNPDAA

sspA

Glutamyl endopeptidase

342 amino acids

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).

Belongs to the peptidase S1B family.

36.977 kDa

MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIKKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA

sspA

Glutamyl endopeptidase

342 amino acids

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).

Belongs to the peptidase S1B family.

36.977 kDa

MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIKKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA

sspA

Glutamyl endopeptidase

336 amino acids

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases.

Belongs to the peptidase S1B family.

36.326 kDa

MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA

sspA

Glutamyl endopeptidase

336 amino acids

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).

Belongs to the peptidase S1B family.

36.313 kDa

MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDTNNSDNPDAA

sspA

Glutamyl endopeptidase

336 amino acids

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases.

Belongs to the peptidase S1B family.

36.326 kDa

MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA

sspA

Glutamyl endopeptidase

333 amino acids

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).

Belongs to the peptidase S1B family.

35.97 kDa

MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQSQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDNPNNPNNPDNPDNGDNNNSDNPDAA

sspA

Glutamyl endopeptidase

327 amino acids

Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).

Belongs to the peptidase S1B family.

35.319 kDa

MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQSQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPNNPDNPDNGDNNNSDNPDAA

sspA

Stringent starvation protein A homolog

214 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme.

Belongs to the GST superfamily. HSP26 family.

24.471 kDa

MTISANKRSVMSLFSDKNDIYSHQVRIVLAEKGVPYELENINPNTISEDFLELNPYANIPTLVDRDLVLFNSRIIMEYLDERFPHPPLMPVYPVLRGKSRLTMHRIEQDWYSLIDIVNKNPESKEAKKALSQLREEMLALGSVFAATSYFMSDEFSLVDCYIAPLLWRMHNLGVQFTGAGGKAIKAYMTKVFQRDSFSQSIGGSAPKHLMDDKE

sspA

Stringent starvation protein A homolog

212 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme.

Belongs to the GST superfamily. HSP26 family.

24.429 kDa

MTSAANKRSIMTLFLDKVDIYCHQVRIVLAEKGVAYATEIVDSESISEDLMELNPYGTIPTLVDRDLVLFNSRIIMEYLDERFPHPPLMPVYPVSRGKSRLLMLRIEQDWYPVLEKAEKGSESERAIALKQLKEEILAIAPVFSQSLYFMSEEFRLVDCYIAPLLWRMQQLGVVFTGTGSKAIKSYMERVFQRDSFLQSVGEMTPKNLMEDK

sspA

Stringent starvation protein A homolog

212 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme.

Belongs to the GST superfamily. HSP26 family.

24.195 kDa

MTSAANKRSIMTLFSDKTDIYCHQVRIVLAEKGVAYETEVVDPQVVSEDLMELNPYGTLPTLVDRDLVLFNSRIIMEYLDERFPHPPLMPVYPVARGKSRLLMLRIEQDWYPVLAKAEKGTDAERAVALKQLREEILAIAPIFTQMPYFMSEEFSLVDCYIAPLLWRMQELGVDFSGAGSKAIKAYMARVFERDSFMQSLGVSAPKNLMDEK

sspA

Stringent starvation protein A

212 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme.

Belongs to the GST superfamily. HSP26 family.

24.305 kDa

MAVAANKRSVMTLFSGPTDIYSHQVRIVLAEKGVSFEIEHVEKDNPPQDLIDLNPNQSVPTLVDRELTLWESRIIMEYLDERFPHPPLMPVYPVARGESRLYMHRIEKDWYTLMNTIINGSASEADAARKQLREELLAIAPVFGQKPYFLSDEFSLVDCYLAPLLWRLPQLGIEFSGPGAKELKGYMTRVFERDSFLASLTEAEREMRLGRS

sspA

Stringent starvation protein A

212 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme.

Belongs to the GST superfamily. HSP26 family.

24.305 kDa

MAVAANKRSVMTLFSGPTDIYSHQVRIVLAEKGVSFEIEHVEKDNPPQDLIDLNPNQSVPTLVDRELTLWESRIIMEYLDERFPHPPLMPVYPVARGESRLYMHRIEKDWYTLMNTIINGSASEADAARKQLREELLAIAPVFGQKPYFLSDEFSLVDCYLAPLLWRLPQLGIEFSGPGAKELKGYMTRVFERDSFLASLTEAEREMRLGRS

sspA

Stringent starvation protein A

212 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme.

Belongs to the GST superfamily. HSP26 family.

24.305 kDa

MAVAANKRSVMTLFSGPTDIYSHQVRIVLAEKGVSFEIEHVEKDNPPQDLIDLNPNQSVPTLVDRELTLWESRIIMEYLDERFPHPPLMPVYPVARGESRLYMHRIEKDWYTLMNTIINGSASEADAARKQLREELLAIAPVFGQKPYFLSDEFSLVDCYLAPLLWRLPQLGIEFSGPGAKELKGYMTRVFERDSFLASLTEAEREMRLGRS

sspA

Stringent starvation protein A

212 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme. It is synthesized predominantly when cells are exposed to amino acid starvation, at which time it accounts for over 50% of the total protein synthesized. It is involved in the transition from P1 early to P1 late gene expression. Rnk and SspA can functionally replace P.aeruginosa alginate regulatory gene algR2.

Belongs to the GST superfamily. HSP26 family.

24.305 kDa

MAVAANKRSVMTLFSGPTDIYSHQVRIVLAEKGVSFEIEHVEKDNPPQDLIDLNPNQSVPTLVDRELTLWESRIIMEYLDERFPHPPLMPVYPVARGESRLYMHRIEKDWYTLMNTIINGSASEADAARKQLREELLAIAPVFGQKPYFLSDEFSLVDCYLAPLLWRLPQLGIEFSGPGAKELKGYMTRVFERDSFLASLTEAEREMRLGRS

sspA

Stringent starvation protein A homolog

212 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme.

Belongs to the GST superfamily. HSP26 family.

24.29 kDa

MSSASSKRSVMTLFSNKDDIYCHQVKIVLAEKGVLYENAEVDLQALPEDLMELNPYGTVPTLVDRDLVLFNSRIIMEYLDERFPHPPLMQVYPVSRAKDRLLMLRIEQDWYPTLAKAENGTEKEKTSALKQLKEELLGIAPIFQQMPYFMNEEFGLVDCYVAPLLWKLKHLGVEFTGTGSKAIKAYMERVFTRDSFLQSVGEAAPKNLMDDK

sspA

Stringent starvation protein A homolog

209 amino acids

Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme.

Belongs to the GST superfamily. HSP26 family.

24.415 kDa

MLKRSIMTLYSGPLDIYSHQVRIVLAEKGVTVDIHNVDANHPSEDLIELNPYATLPTLVDRDLVLFESRVIMEYLDERFPHPPLLPVYPVARSRCRLLMYRIERNFYHSMKIIEEGTPKQAETEREFLTKELIELDPVFGEKTYFMNDDFTLVDCVMAPLLWRLPHLGVHVPPRAAKSMYKYKKLIFERESFKASLSESESELREVDGI

sspA

Small, acid-soluble spore protein A

69 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.

7.071 kDa

MANNNSGNSNNLLVPGAAQAIDQMKLEIASEFGVNLGADTTSRANGSVGGEITKRLVSFAQQNMGGGQF

sspA

Small, acid-soluble spore protein gamma-type

54 amino acids

SASP are proteins degraded in the first minutes of spore germination and provide amino acids for both new protein synthesis and metabolism. These proteins may be involved in dormant spore's high resistance to UV light.

Belongs to the gamma-type SASP family.

6.343 kDa

MAKKNRNKQQQEMQQQQQQHQAEFANEFAEGSSAEQARQQQQKAAGKRQKKNQQ