Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P13423 (PAG_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protective antigen

Short name=PA
Alternative name(s):
Anthrax toxins translocating protein
PA-83
Short name=PA83

Cleaved into the following 2 chains:

  1. Protective antigen PA-20
    Short name=PA20
  2. Protective antigen PA-63
    Short name=PA63
Gene names
Name:pagA
Synonyms:pag
Ordered Locus Names:pXO1-110, BXA0164, GBAA_pXO1_0164
Encoded onPlasmid pXO1
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax.

Subunit structure

Anthrax toxins are composed of three distinct proteins, a protective antigen (PA), a lethal factor (LF) and an edema factor (EF). None of these is toxic by itself. PA+LF forms the lethal toxin (LeTx); PA+EF forms the edema toxin (EdTx). PA-63 forms heptamers and this oligomerization is required for LF or EF binding. This complex is endocytosed by the host. Once activated, at low pH, the heptamer undergoes conformational changes and converts from prepore to pore inserted in the membrane, forming cation-selective channels and triggering the release of LF and EF in the host cytoplasm.

Subcellular location

Secretedextracellular space. Note: Secreted through the Sec-dependent secretion pathway. Therefore, PA is translocated across the membrane in an unfolded state and then it is folded into its native configuration on the trans side of the membrane, prior to its release to the environment. PA requires the extracellular chaperone PrsA for efficient folding.

Domain

The molecule is folded into four functional domains. Each domain is required for a particular step in the toxicity process. Domain 1 contains two calcium ions and the proteolytic activation site. Cleavage of the PA monomer releases the subdomain 1a, which is the N-terminal fragment of 20-kDa (PA20). The subdomain 1b is part of the remaining 63-kDa fragment (PA63) and contains the binding sites for LP and EF. Domain 2 is a beta-barrel core containing a large flexible loop that has been implicated in membrane insertion and pore formation. There is a chymotrypsin cleavage site in this loop that is required for toxicity. Domain 3 has a hydrophobic patch thought to be involved in protein-protein interactions. Domain 4 appears to be a separate domain and shows limited contact with the other three domains: it would swing out of the way during membrane insertion. It is required for binding to the receptor; the small loop is involved in receptor recognition. Ref.9 Ref.16

Post-translational modification

Proteolytic activation by furin or a furin-like protease cleaves the protein in two parts, PA-20 and PA-63; the latter is the mature protein. The cleavage occurs at the cell surface and probably in the serum of infected animals as well; both native and cleaved PA are able to bind to the cell receptor. The release of PA20 from the remaining receptor-bound PA63 exposes the binding site for EF and LF, and promotes oligomerization and internalization of the protein.

Miscellaneous

In Ref.16 multiple mutagenesis experiments were performed that showed that the residues present in the small loop of domain 4, and not the ones in the large loop, are involved in receptor recognition. In Ref.23 high-throughput scanning mutagenesis experiments were performed in which all residues of PA-63 were mutated into Cys. Dominantly negative (DN) mutants were all clustered in domain 2. DN mutants prevent the conformational transition of PA-63 from the prepore to the pore state.

Sequence similarities

Belongs to the bacterial binary toxin family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionToxin
   PTMCleavage on pair of basic residues
   Technical term3D-structure
Complete proteome
Plasmid
Reference proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 15044490Ref.27. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16762926. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-456868,EBI-456868
ANTXR1Q9H6X2-23EBI-456868,EBI-905659From a different organism.
ANTXR2P583357EBI-456868,EBI-456840From a different organism.
lefP159175EBI-456868,EBI-456923

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 764735Protective antigen
PRO_0000021996
Chain30 – 196167Protective antigen PA-20
PRO_0000021997
Chain197 – 764568Protective antigen PA-63
PRO_0000021998

Regions

Region30 – 287258Domain 1, calcium-binding; LF and EF binding sites
Region288 – 516229Domain 2, membrane insertion and heptamerization
Region517 – 624108Domain 3, heptamerization
Region625 – 764140Domain 4, binding to the receptor

Sites

Metal binding2061Calcium
Metal binding2081Calcium
Metal binding2101Calcium
Metal binding2171Calcium
Site196 – 1972Cleavage; by furin
Site343 – 3442Cleavage; by chymotrypsin; required for translocation of LF and EF
Site7121Essential for binding to cell receptor

Natural variations

Natural variant2951M → I in strain: PAI.
Natural variant3921N → D in strain: PAI.
Natural variant5601F → L in Sverdlovsk sample.
Natural variant5651P → S in strain: BA1024.
Natural variant6001A → V in strain: BA1024, V770-NP1-R, Carbosap and Ferrara.

Experimental info

Mutagenesis2131P → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. Ref.16 Ref.22
Mutagenesis2161L → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. Ref.16 Ref.22
Mutagenesis2311F → A: Loss of ability to bind to LF and completely nontoxic. Ref.16 Ref.22
Mutagenesis2321L → A: Loss of ability to bind to LF and completely nontoxic. Ref.16 Ref.22
Mutagenesis2341P → A: Loss of ability to bind to LF and completely nontoxic. Ref.16 Ref.22
Mutagenesis2361I → A: Loss of ability to bind to LF and completely nontoxic. Ref.16 Ref.22
Mutagenesis2391I → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. Ref.16 Ref.22
Mutagenesis2551W → A: No effect on LF-binding ability and as toxic as the wild-type. Ref.16 Ref.22
Mutagenesis2651F → A: No effect on LF-binding ability and as toxic as the wild-type. Ref.16 Ref.22
Mutagenesis2891P → A: Reduced toxicity in combination with lethal factor. Decreased membrane insertion and translocation of LF. Ref.16 Ref.19
Mutagenesis342 – 3443FFD → AAA: Decrease in toxicity probably due to slow translocation of LF. Ref.15 Ref.16
Mutagenesis342 – 3432Missing: Loss of toxicity probably due to loss of capability to translocate LF. Ref.16
Mutagenesis3421F → C: Loss of toxicity probably due to loss of capability to translocate LF. Ref.16
Mutagenesis3441D → A: Decrease in toxicity probably due to slow translocation of LF. Ref.15 Ref.16
Mutagenesis3751W → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. Ref.16 Ref.17
Mutagenesis3791M → A: No effect. Ref.16 Ref.17
Mutagenesis3811L → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. Ref.16 Ref.17
Mutagenesis3931I → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.23
Mutagenesis4091T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.23
Mutagenesis4111S → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.23
Mutagenesis4221T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.23
Mutagenesis4261K → A or D: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.21 Ref.23
Mutagenesis4281N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.23
Mutagenesis4401Y → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.23
Mutagenesis4511N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.23
Mutagenesis4541D → A or K: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.21 Ref.23
Mutagenesis4561F → A: Loss of capability to undergo conformational changes that lead to pore formation and translocation. Ref.16 Ref.21 Ref.23
Mutagenesis5121Q → A: Loss of heptamerization capability. Ref.16 Ref.20
Mutagenesis5411D → A: Loss of heptamerization capability. Ref.16 Ref.20
Mutagenesis5431L → A: Decrease in heptamerization capability. Ref.16 Ref.20
Mutagenesis5811F → A: Loss of toxicity due to defective oligomerization. Ref.16 Ref.18
Mutagenesis5831F → A: Decrease in toxicity due to defective oligomerization. Ref.16 Ref.18
Mutagenesis5911I → A: Loss of toxicity due to defective oligomerization. Ref.16 Ref.18
Mutagenesis5951L → A: Loss of toxicity due to defective oligomerization. Ref.16 Ref.18
Mutagenesis6031I → A: Loss of toxicity due to defective oligomerization. Ref.16 Ref.18
Mutagenesis6211R → A: No effect. Ref.16 Ref.20
Mutagenesis6861N → A: Decrease in toxicity due to decrease in cell binding. Ref.16 Ref.24
Mutagenesis7081K → A: No effect on toxicity. Ref.16 Ref.24
Mutagenesis7091K → A: Slight decrease in toxicity. Ref.16 Ref.24
Mutagenesis7101Y → A: Great decrease in toxicity due to decrease in cell binding. Ref.16 Ref.24
Mutagenesis7111N → A: Loss of toxicity due to decrease in cell binding. Ref.16 Ref.24
Mutagenesis7121D → A: Loss of toxicity due to decrease in cell binding. Ref.16 Ref.24
Mutagenesis7131K → A: No effect on toxicity. Ref.16 Ref.24
Mutagenesis7141L → A: No effect on toxicity. Ref.16 Ref.24
Mutagenesis7151P → A: Great decrease in toxicity due to decrease in cell binding. Ref.16 Ref.24
Mutagenesis7161L → A: Decrease in toxicity due to decrease in cell binding. Ref.16 Ref.24
Mutagenesis7171Y → A: No effect on toxicity. Ref.16 Ref.24
Mutagenesis7181I → A: Decrease in toxicity due to decrease in cell binding. Ref.16 Ref.24
Mutagenesis7191S → A: No effect on toxicity. Ref.16
Mutagenesis7201N → A: No effect on toxicity. Ref.16 Ref.24
Mutagenesis7211P → A: No effect on toxicity. Ref.16 Ref.24
Mutagenesis7221N → A: No effect on toxicity. Ref.16 Ref.24
Sequence conflict3141Q → E in AAA22637. Ref.1

Secondary structure

............................................................................................................................................................. 764
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13423 [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: 3AE1EFBF48FAA03F

FASTA76485,811
        10         20         30         40         50         60 
MKKRKVLIPL MALSTILVSS TGNLEVIQAE VKQENRLLNE SESSSQGLLG YYFSDLNFQA 

        70         80         90        100        110        120 
PMVVTSSTTG DLSIPSSELE NIPSENQYFQ SAIWSGFIKV KKSDEYTFAT SADNHVTMWV 

       130        140        150        160        170        180 
DDQEVINKAS NSNKIRLEKG RLYQIKIQYQ RENPTEKGLD FKLYWTDSQN KKEVISSDNL 

       190        200        210        220        230        240 
QLPELKQKSS NSRKKRSTSA GPTVPDRDND GIPDSLEVEG YTVDVKNKRT FLSPWISNIH 

       250        260        270        280        290        300 
EKKGLTKYKS SPEKWSTASD PYSDFEKVTG RIDKNVSPEA RHPLVAAYPI VHVDMENIIL 

       310        320        330        340        350        360 
SKNEDQSTQN TDSQTRTISK NTSTSRTHTS EVHGNAEVHA SFFDIGGSVS AGFSNSNSST 

       370        380        390        400        410        420 
VAIDHSLSLA GERTWAETMG LNTADTARLN ANIRYVNTGT APIYNVLPTT SLVLGKNQTL 

       430        440        450        460        470        480 
ATIKAKENQL SQILAPNNYY PSKNLAPIAL NAQDDFSSTP ITMNYNQFLE LEKTKQLRLD 

       490        500        510        520        530        540 
TDQVYGNIAT YNFENGRVRV DTGSNWSEVL PQIQETTARI IFNGKDLNLV ERRIAAVNPS 

       550        560        570        580        590        600 
DPLETTKPDM TLKEALKIAF GFNEPNGNLQ YQGKDITEFD FNFDQQTSQN IKNQLAELNA 

       610        620        630        640        650        660 
TNIYTVLDKI KLNAKMNILI RDKRFHYDRN NIAVGADESV VKEAHREVIN SSTEGLLLNI 

       670        680        690        700        710        720 
DKDIRKILSG YIVEIEDTEG LKEVINDRYD MLNISSLRQD GKTFIDFKKY NDKLPLYISN 

       730        740        750        760 
PNYKVNVYAV TKENTIINPS ENGDTSTNGI KKILIFSKKG YEIG 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis."
Welkos S.L., Lowe J.R., Eden-Mccutchan F., Vodkin M., Leppla S.H., Schmidt J.J.
Gene 69:287-300(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genetic diversity in the protective antigen gene of Bacillus anthracis."
Price L.B., Hugh-Jones M., Jackson P.J., Keim P.
J. Bacteriol. 181:2358-2362(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 28, 33, BA1024 and BA1035.
[3]"Attenuated nontoxinogenic and nonencapsulated recombinant Bacillus anthracis spore vaccines protect against anthrax."
Cohen S., Mendelson I., Altboum Z., Kobiler D., Elhanany E., Bino T., Leitner M., Inbar I., Rosenberg H., Gozes Y., Barak R., Fisher M., Kronman C., Velan B., Shafferman A.
Infect. Immun. 68:4549-4558(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: V770-NP1-R / ATCC 14185.
[4]"Sequence and organization of pXO1, the large Bacillus anthracis plasmid harboring the anthrax toxin genes."
Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., Keim P., Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., Martinez Y., Ricke D., Svensson R., Jackson P.J.
J. Bacteriol. 181:6509-6515(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[5]"Comparative genome sequencing for discovery of novel polymorphisms in Bacillus anthracis."
Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L., Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P., Fraser C.M.
Science 296:2028-2033(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Ames / isolate Florida / A2012.
[6]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[7]"Sequence analysis of the genes encoding for the major virulence factors of Bacillus anthracis vaccine strain 'Carbosap'."
Adone R., Pasquali P., La Rosa G., Marianelli C., Muscillo M., Fasanella A., Francia M., Ciuchini F.
J. Appl. Microbiol. 93:117-121(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-751.
Strain: Carbosap and Ferrara.
[8]"Preparation of a positive control DNA for molecular diagnosis of Bacillus anthracis."
Inoue S., Noguchi A., Tanabayashi K., Yamada A.
Jpn. J. Infect. Dis. 57:29-32(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-434.
Strain: PAI.
[9]"The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity."
Singh Y., Klimpel K.R., Quinn C.P., Chaudhary V.K., Leppla S.H.
J. Biol. Chem. 266:15493-15497(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.
[10]"Anthrax protective antigen forms oligomers during intoxication of mammalian cells."
Milne J.C., Furlong D., Hanna P.C., Wall J.S., Collier R.J.
J. Biol. Chem. 269:20607-20612(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: Sterne.
[11]"Proteolytic activation of receptor-bound anthrax protective antigen on macrophages promotes its internalization."
Beauregard K.E., Collier R.J., Swanson J.A.
Cell. Microbiol. 2:251-258(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[12]"Regulation of the Bacillus anthracis protective antigen gene: CO2 and a trans-acting element activate transcription from one of two promoters."
Koehler T.M., Dai Z., Kaufman-Yarbray M.
J. Bacteriol. 176:586-595(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: TOXIN REGULATION.
Strain: Weybridge.
[13]"Production of Bacillus anthracis protective antigen is dependent on the extracellular chaperone, PrsA."
Williams R.C., Rees M.L., Jacobs M.F., Pragai Z., Thwaite J.E., Baillie L.W., Emmerson P.T., Harwood C.R.
J. Biol. Chem. 278:18056-18062(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FOLDING BY PSRA.
[14]"Binding of anthrax toxin to its receptor is similar to alpha integrin-ligand interactions."
Bradley K.A., Mogridge J., Jonah G., Rainey G.J.A., Batty S., Young J.A.T.
J. Biol. Chem. 278:49342-49347(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANTHRAX TOXIN RECEPTOR.
[15]"The chymotrypsin-sensitive site, FFD315, in anthrax toxin protective antigen is required for translocation of lethal factor."
Singh Y., Klimpel K.R., Arora N., Sharma M., Leppla S.H.
J. Biol. Chem. 269:29039-29046(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 342-PHE-PHE-343 AND ASP-344.
Strain: Sterne.
[16]"Identification of a receptor-binding region within domain 4 of the protective antigen component of anthrax toxin."
Varughese M., Teixeira A.V., Liu S., Leppla S.H.
Infect. Immun. 67:1860-1865(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF DOMAIN 4 LOOPS.
Strain: Sterne.
[17]"Trp 346 and Leu 352 residues in protective antigen are required for the expression of anthrax lethal toxin activity."
Batra S., Gupta P., Chauhan V., Singh A., Bhatnagar R.
Biochem. Biophys. Res. Commun. 281:186-192(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-375; MET-379 AND LEU-381.
Strain: Sterne.
[18]"Hydrophobic residues Phe552, Phe554, Ile562, Leu566, and Ile574 are required for oligomerization of anthrax protective antigen."
Ahuja N., Kumar P., Bhatnagar R.
Biochem. Biophys. Res. Commun. 287:542-549(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PHE-581; PHE-583; ILE-591; LEU-595 AND ILE-603.
Strain: Sterne.
[19]"Role of residues constituting the 2beta1 strand of domain II in the biological activity of anthrax protective antigen."
Khanna H., Chopra A.P., Arora N., Chaudhry A., Singh Y.
FEMS Microbiol. Lett. 199:27-31(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-289.
Strain: Sterne.
[20]"Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin."
Mogridge J., Mourez M., Collier R.J.
J. Bacteriol. 183:2111-2116(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLN-512; ASP-541; LEU-543 AND ARG-621.
[21]"Point mutations in anthrax protective antigen that block translocation."
Sellman B.R., Nassi S., Collier R.J.
J. Biol. Chem. 276:8371-8376(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-426; ASP-454 AND PHE-456.
[22]"Identification of amino acid residues of anthrax protective antigen involved in binding with lethal factor."
Chauhan V., Bhatnagar R.
Infect. Immun. 70:4477-4484(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-213; LEU-216; PHE-231; LEU-232; PRO-234; ILE-236; ILE-239; TRP-255 AND PHE-265.
Strain: Sterne.
[23]"Mapping dominant-negative mutations of anthrax protective antigen by scanning mutagenesis."
Mourez M., Yan M., Lacy D.B., Dillon L., Bentsen L., Marpoe A., Maurin C., Hotze E., Wigelsworth D., Pimental R.-A., Ballard J.D., Collier R.J., Tweten R.K.
Proc. Natl. Acad. Sci. U.S.A. 100:13803-13808(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ILE-393; THR-409; SER-411; THR-422; LYS-426; ASN-428; TYR-440; ASN-451; ASP-454 AND PHE-456.
[24]"Alanine-scanning mutations in domain 4 of anthrax toxin protective antigen reveal residues important for binding to the cellular receptor and to a neutralizing monoclonal antibody."
Rosovitz M.J., Schuck P., Varughese M., Chopra A.P., Mehra V., Singh Y., McGinnis L.M., Leppla S.H.
J. Biol. Chem. 278:30936-30944(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-686; LYS-708; LYS-709; TYR-710; ASN-711; ASP-712; LYS-713; LEU-714; PRO-715; LEU-716; TYR-717; ILE-718; ASN-720; PRO-721 AND ASN-722.
[25]"Crystal structure of the anthrax toxin protective antigen."
Petosa C., Collier R.J., Klimpel K.R., Leppla S.H., Liddington R.C.
Nature 385:833-838(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[26]"Crystal structure of a complex between anthrax toxin and its host cell receptor."
Santelli E., Bankston L.A., Leppla S.H., Liddington R.C.
Nature 430:905-908(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-764 IN COMPLEX WITH ANTXR2.
[27]"Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation."
Lacy D.B., Wigelsworth D.J., Melnyk R.A., Harrison S.C., Collier R.J.
Proc. Natl. Acad. Sci. U.S.A. 101:13147-13151(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.3 ANGSTROMS) OF 203-764 IN COMPLEX WITH ANTXR2.
[28]"Anthrax."
Mock M., Fouet A.
Annu. Rev. Microbiol. 55:647-671(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22589 Genomic DNA. Translation: AAA22637.1.
AF306778 Genomic DNA. Translation: AAG24446.1.
AF306779 Genomic DNA. Translation: AAG24447.1.
AF306780 Genomic DNA. Translation: AAG24448.1.
AF306781 Genomic DNA. Translation: AAG24449.1.
AF306782 Genomic DNA. Translation: AAG24450.1.
AF306783 Genomic DNA. Translation: AAG24451.1.
AF268967 Genomic DNA. Translation: AAF86457.1.
AF065404 Genomic DNA. Translation: AAD32414.1.
AE011190 Genomic DNA. Translation: AAM26109.1.
AE017336 Genomic DNA. Translation: AAT28905.2.
AJ413936 Genomic DNA. Translation: CAC93934.1.
AJ413937 Genomic DNA. Translation: CAC93935.1.
AB125961 Genomic DNA. Translation: BAD14937.1.
PIRI39934.
RefSeqNP_052806.1. NC_001496.1.
NP_652920.1. NC_003980.1.
YP_016495.2. NC_007322.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACCX-ray2.10A30-764[»]
1T6BX-ray2.50X30-764[»]
1TX5model-C30-764[»]
1TZNX-ray4.30A/B/C/D/E/F/G/H/I/J/K/L/M/O203-764[»]
1TZOX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L/M/O203-764[»]
1V36model-A/B/C/D/E/F/G197-764[»]
3ETBX-ray3.80J/K/L/M621-764[»]
3INOX-ray1.95A/B624-764[»]
3KWVX-ray3.10A/B/D/E197-764[»]
3MHZX-ray1.70A30-764[»]
3Q8AX-ray3.13A30-764[»]
3Q8BX-ray2.00A30-764[»]
3Q8CX-ray2.85A30-764[»]
3Q8EX-ray2.10A30-764[»]
3Q8FX-ray2.10A30-764[»]
3TEWX-ray1.45A30-764[»]
3TEXX-ray1.70A30-764[»]
3TEYX-ray2.12A30-764[»]
3TEZX-ray1.83A30-764[»]
4EE2X-ray1.91A30-764[»]
4H2AX-ray1.62A30-764[»]
4NAMX-ray1.70A30-764[»]
ProteinModelPortalP13423.
SMRP13423. Positions 45-764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29841N.
IntActP13423. 15 interactions.
MINTMINT-7014733.
STRING261594.GBAA_pXO1_0164.

Chemistry

ChEMBLCHEMBL5352.

Protein family/group databases

TCDB1.C.42.1.1. the channel-forming bacillus anthracis protective antigen (bapa) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT28905; AAT28905; GBAA_pXO1_0164.
GeneID1158723.
2820165.
3361714.
KEGGbar:GBAA_pXO1_0164.
PATRIC24662127. VBIBacAnt106580_0153.

Phylogenomic databases

eggNOGNOG284171.
HOGENOMHOG000034566.
KOK11030.
OMAGFNESNG.
OrthoDBEOG6D5FXS.

Enzyme and pathway databases

BioCycANTHRA:GBAA_PXO1_0164-MONOMER.
BANT261594:GJ7F-5750-MONOMER.

Family and domain databases

Gene3D2.60.120.240. 1 hit.
2.60.40.810. 1 hit.
3.10.20.110. 1 hit.
3.90.182.10. 1 hit.
InterProIPR003896. Bacterial_exotoxin_B.
IPR023125. Bacterial_exotoxin_B_Fd-like.
IPR011658. PA14.
IPR027441. PA_dom4.
IPR027439. PA_heptamer_dom.
[Graphical view]
PfamPF03495. Binary_toxB. 1 hit.
PF07691. PA14. 1 hit.
[Graphical view]
PRINTSPR01391. BINARYTOXINB.
SMARTSM00758. PA14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13423.
PMAP-CutDBP13423.

Entry information

Entry namePAG_BACAN
AccessionPrimary (citable) accession number: P13423
Secondary accession number(s): Q937W2 expand/collapse secondary AC list , Q937W3, Q9F5R7, Q9KH69, Q9RQU2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 18, 2001
Last modified: June 11, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references