DP00157: Cell invasion protein sipAFASTA viewXML view

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



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.

Region 1: 425-512 Region 2: 513-657 Region 3: 658-684

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.


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:
  1. X-ray crystallography

  2. Rotory shadowing electron microscopy

  3. Sensitivity to proteolysis

References:
  1. 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:
 



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:
  1. X-ray crystallography

  2. Rotory shadowing electron microscopy

  3. Sensitivity to proteolysis

References:
  1. 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:
 



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:
  1. X-ray crystallography

  2. Rotory shadowing electron microscopy

  3. Sensitivity to proteolysis

References:
  1. 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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