General information | DisProt: | DP00157 | Name: | Cell invasion protein sipA | Synonym(s): | SIPA_SALTY
Effector protein sipA
| First appeared in release: | Release 1.1 (12/01/2003) | UniProt: | Q56027 | UniGene: | | SwissProt: | SIPA_SALTY | TrEMBL: | | NCBI (GI): | 62903507 | Source organism: | Salmonella typhimurium | Sequence length: | 684 | Percent disordered: | 17% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MVTSVRTQPP VIMPGMQTEI KTQATNLAAN LSAVRAKCHS DAVREIKGPQ LEDFPALIKQ - 60 ASLDALFKCG KDAEALKEVF TNSNNVAGKK AIMEFAGLFR SALNATSDSP EAKTLLMKVG - 120 AEYAAQIIKD GLKEKSAFGP WLPETKKAEA KLENLEKQLL DIIKNNTGGE LSKLSTNLVM - 180 QEVMPYIASC IEHNFGCTLD PLTRSNLTHL VDKAAAKAVE ALDMCPQKLT QEQGTSVGRE - 240 ARHLEMQTLI PLLLRNVFAQ IPADKLPDPK IPEPAAGPVP DGGKKAEPTG INININIDSS - 300 NHSVDNSKHI NNAEPVDNGQ RHIDNSNHDN SRKTIDNSRT FIDNSQRNGE SHHSTNSSNV - 360 SHSHSRVDST THQTETAHSA STGAIDHGIA GKIDVTAHAT AEAVTNASSE SKDGKVVTSE - 420 KGTTGETTSF DEVDGVTSKS IIGKPVQATV HGVDDNKQQS QTAEIVNVKP LASQLAGVEN - 480 VKTDTLQSDT TVITGNKAGT TDNDNSQTDK TGPFSGLKFK QNSFLSTVPS VTNMHSMHFD - 540 ARETFLGVIR KALEPDTSTP FPVRRAFDGL RAEILPNDTI KSAALKAQCS DIDKHPELKA - 600 KMETLKEVIT HHPQKEKLAE IALQFAREAG LTRLKGETDY VLSNVLDGLI GDGSWRAGPA - 660 YESYLNKPGV DRVITTVDGL HMQR
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Functional narrative |
Salmonella SipA invasion protein binds host actin and promotes its polymerization thus contributing to the host cytoskeletal rearrangements that serve to internalize the pathogen. The C-terminal domain has been termed a "molecular staple" comprised of a globular domain and two non-globular arms. The arms reach out and tether the actin molecules on opposing strands. Once the host actin is bound, polymerization occurs. SipA causes more than 1 billion new human infections per year and represents a potential biodefense food and water safety threat. SipA sequence and structure differ from other actin tethering host molecules (ie: nebulin), an example of convergent evolution in bacterial pathogenesis.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered - Extended | Name: | | Location: | 425 - 512 | Length: | 88 | Region sequence: |
GETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTD TLQSDTTVITGNKAGTTDNDNSQTDKTG | Modification type: | Engineered
Fragment
| PDB: | 1Q5Z:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular assembly
| Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography
- Rotory shadowing electron microscopy
- Sensitivity to proteolysis
| References:
- Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. "Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms." Science. 2003; 301(5641): 1918-1921. PubMed: 14512630
| Comments:
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Region 2 | Type: | Ordered | Name: | | Location: | 513 - 657 | Length: | 145 | Region sequence: |
PFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRA EILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLT RLKGETDYVLSNVLDGLIGDGSWRA | Modification type: | Engineered
Fragment
| PDB: | 1Q5Z:A | Structural/functional type: | Function arises from the ordered state | Functional classes: | Molecular assembly
| Functional subclasses: | Polymerization
| Detection methods:
- X-ray crystallography
- Rotory shadowing electron microscopy
- Sensitivity to proteolysis
| References:
- Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. "Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms." Science. 2003; 301(5641): 1918-1921. PubMed: 14512630
| Comments:
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Region 3 | Type: | Disordered - Extended | Name: | | Location: | 658 - 684 | Length: | 27 | Region sequence: |
GPAYESYLNKPGVDRVITTVDGLHMQR | Modification type: | Engineered
Fragment
| PDB: | 1Q5Z:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular assembly
| Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography
- Rotory shadowing electron microscopy
- Sensitivity to proteolysis
| References:
- Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. "Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms." Science. 2003; 301(5641): 1918-1921. PubMed: 14512630
| Comments:
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