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1.C.73.1.1
Pore-forming exotoxin A (chain A; ExlA)  (Rasper and Merrill 1994; Méré et al., 2005).  Pore-formation has been demonstrated (Zalman and Wisnieski 1985).  Secretion depends on ExlB, a Two Partner Secretion (TPS; TC# 1.B.20) system, as well as type IV pili.  The protein has three domains: an N-terminal hemolyin domain, a central RGD motif domain, and a C-terminal domain required for cell lysis.  Pore-formation precedes lysis (Basso et al. 2017). ExlA triggers cadherin cleavage by promoting calcium influx which activates ADAM10 for proteolysis (Reboud et al. 2017).

Accession Number:P11439
Protein Name:Exotoxin A
Length:638
Molecular Weight:69284.00
Species:Pseudomonas aeruginosa [287]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate small molecules

Cross database links:

HEGENOM: HBG639690
RefSeq: NP_249839.1   
Entrez Gene ID: 877850   
Pfam: PF09101    PF09009    PF09102   
Drugbank: Drugbank Link   
BioCyc: PAER208964:PA1148-MONOMER   
KEGG: pae:PA1148   

Gene Ontology

GO:0016757 F:transferase activity, transferring glycosyl...
GO:0009405 P:pathogenesis

References (8)

[1] “Cloning, nucleotide sequence, and expression in Escherichia coli of the exotoxin A structural gene of Pseudomonas aeruginosa.”  Gray G.L.et.al.   6201861
[2] “Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.”  Stover C.K.et.al.   10984043
[3] “Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is photolabeled by NAD and shows functional homology with glutamic acid 148 of diphtheria toxin.”  Carroll S.F.et.al.   2885323
[4] “Mutagenesis of Pseudomonas exotoxin in identification of sequences responsible for the animal toxicity.”  Chaudhary V.K.et.al.   2118903
[5] “Biochemical and immunochemical studies of proteolytic fragments of exotoxin A from Pseudomonas aeruginosa.”  Bourdenet S.et.al.   2170123
[6] “Reduction of furin-nicked Pseudomonas exotoxin A: an unfolding story.”  McKee M.L.et.al.   10600112
[7] “The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin.”  Li M.et.al.   7568123
[8] “Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: implications for the activation process and for ADP ribosylation.”  Li M.et.al.   8692916
Structure:
1AER   1DMA   1IKP   1IKQ   1XK9   1ZM2   1ZM3   1ZM4   1ZM9   2ZIT   [...more]

External Searches:

  • Search: DB with
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  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MHLTPHWIPL VASLGLLAGG SFASAAEEAF DLWNECAKAC VLDLKDGVRS SRMSVDPAIA 
61:	DTNGQGVLHY SMVLEGGNDA LKLAIDNALS ITSDGLTIRL EGGVEPNKPV RYSYTRQARG 
121:	SWSLNWLVPI GHEKPSNIKV FIHELNAGNQ LSHMSPIYTI EMGDELLAKL ARDATFFVRA 
181:	HESNEMQPTL AISHAGVSVV MAQAQPRREK RWSEWASGKV LCLLDPLDGV YNYLAQQRCN 
241:	LDDTWEGKIY RVLAGNPAKH DLDIKPTVIS HRLHFPEGGS LAALTAHQAC HLPLETFTRH 
301:	RQPRGWEQLE QCGYPVQRLV ALYLAARLSW NQVDQVIRNA LASPGSGGDL GEAIREQPEQ 
361:	ARLALTLAAA ESERFVRQGT GNDEAGAASA DVVSLTCPVA AGECAGPADS GDALLERNYP 
421:	TGAEFLGDGG DISFSTRGTQ NWTVERLLQA HRQLEERGYV FVGYHGTFLE AAQSIVFGGV 
481:	RARSQDLDAI WRGFYIAGDP ALAYGYAQDQ EPDARGRIRN GALLRVYVPR SSLPGFYRTG 
541:	LTLAAPEAAG EVERLIGHPL PLRLDAITGP EEEGGRLETI LGWPLAERTV VIPSAIPTDP 
601:	RNVGGDLDPS SIPDKEQAIS ALPDYASQPG KPPREDLK