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sipA

Gene
sipA
Protein
Cell invasion protein SipA
Organism
Salmonella enteritidis
Length
685 amino acids
Function
Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity).
Similarity
Belongs to the SipA/IpaA family.
Mass
73.972 kDa
Sequence
MVTSVRTQPPVIMPGMQTEIKTQATNLAANLSAVRESATTTLSGEIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCHQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGINININIDSSNHSVDNSKHINNSRSHVDNSQRHIDNSNHDNSRKTIDNSRTFIDNSQRNGESHHSTNSSNVSHSHSRVDSTTHQTETAHSASTGAIDHGIAGKIDVTAHATAEAVTNASSESKDGKVVTSEKGTTGETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR

Gene
sipA
Protein
Cell invasion protein SipA
Organism
Salmonella typhi
Length
685 amino acids
Function
Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization (By similarity).
Similarity
Belongs to the SipA/IpaA family.
Mass
73.94 kDa
Sequence
MVTSVRTQPPVIMPGMQTEIKTQATNLAANLSAVRESATATLSGEIKGQQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSSLTQLVDKAAAKAVEALDMCHQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGINININIDSSNHSVDNSKHINNSRSHVDNSQRHIDNSNHDNSRKTIDNSRTFIDNSQRHGESHHSTNSSNVSHSHSRVDSTTHQTETAHSASTGTIDHGIAGKIDVTAHATAEAVTNSSSESKDGKVVTSEKGTTGETTSFDEVDGVTSKSIIGKPLQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKIDTLQSDSTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSIHFNAREAFLGVIRKALEPDASTPFPVRRAFDGLRGEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRQKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR

Gene
sipA
Protein
Cell invasion protein sipA
Organism
Salmonella typhimurium (strain SL1344)
Length
685 amino acids
Function
Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments.
Similarity
Belongs to the SipA/IpaA family.
Mass
73.942 kDa
Sequence
MVTSVRTQPPVIMPGMQTEIKTQATNLAANLSAVRESATATLSGEIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCHQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGINININIDSSNHSVDNSKHINNSRSHVDNSQRHIDNSNHDNSRKTIDNSRTFIDNSQRNGESHHSTNSSNVSHSHSRVDSTTHQTETAHSASTGAIDHGIAGKIDVTAHATAEAVTNASSESKDGKVVTSEKGTTGETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR

Gene
sipA
Protein
Cell invasion protein SipA
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
685 amino acids
Function
Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments.
Similarity
Belongs to the SipA/IpaA family.
Mass
73.942 kDa
Sequence
MVTSVRTQPPVIMPGMQTEIKTQATNLAANLSAVRESATATLSGEIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCHQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGINININIDSSNHSVDNSKHINNSRSHVDNSQRHIDNSNHDNSRKTIDNSRTFIDNSQRNGESHHSTNSSNVSHSHSRVDSTTHQTETAHSASTGAIDHGIAGKIDVTAHATAEAVTNASSESKDGKVVTSEKGTTGETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR

Gene
sipA
Protein
Signal peptidase I
Organism
Bacillus amyloliquefaciens
Length
185 amino acids
Similarity
Belongs to the peptidase S26 family.
Mass
21.104 kDa
Sequence
MKSEKEKTSKKSAVLDWAKAIIIAVVLAVLIRNFLFAPYVVDGESMEPTLHDRERIFVNMTVKYISDFKRGQIVVLNGENEHYVKRIIGLPGDTVQMKNDQLYINGKKVSEPYLAANKKKAKQDGYTLTDDFGPVKVPDDKYFVMGDNRRNSMDSRNGLGLFTKKQIAGTSKFVFFPFNEIRKTK

Gene
sipA
Protein
Signal peptidase I
Organism
Bacillus amyloliquefaciens
Length
185 amino acids
Similarity
Belongs to the peptidase S26 family.
Mass
21.104 kDa
Sequence
MKSEKEKTSKKSAVLDWAKAIIIAVVLAVLIRNFLFAPYVVDGESMEPTLHDRERIFVNMTVKYISDFKRGQIVVLNGENEHYVKRIIGLPGDTVQMKNDQLYINGKKVSEPYLAANKKKAKQDGYTLTDDFGPVKVPDDKYFVMGDNRRNSMDSRNGLGLFTKKQIAGTSKFVFFPFNEIRKTK