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P13423

- PAG_BACAN

UniProt

P13423 - PAG_BACAN

Protein

Protective antigen

Gene

pagA

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (18 Oct 2001)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei196 – 1972Cleavage; by furin
    Metal bindingi206 – 2061Calcium
    Metal bindingi208 – 2081Calcium
    Metal bindingi210 – 2101Calcium
    Metal bindingi217 – 2171Calcium
    Sitei343 – 3442Cleavage; by chymotrypsin; required for translocation of LF and EF
    Sitei712 – 7121Essential for binding to cell receptor

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW
    2. protein homooligomerization Source: InterPro

    Keywords - Molecular functioni

    Toxin

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

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

    Protein family/group databases

    TCDBi1.C.42.1.1. the channel-forming bacillus anthracis protective antigen (bapa) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protective antigen
    Short name:
    PA
    Alternative name(s):
    Anthrax toxins translocating protein
    PA-83
    Short name:
    PA83
    Cleaved into the following 2 chains:
    Protective antigen PA-20
    Short name:
    PA20
    Protective antigen PA-63
    Short name:
    PA63
    Gene namesi
    Name:pagA
    Synonyms:pag
    Ordered Locus Names:pXO1-110, BXA0164, GBAA_pXO1_0164
    Encoded oniPlasmid pXO10 Publication
    OrganismiBacillus anthracis
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000594: Plasmid pXO1

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131P → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 2 Publications
    Mutagenesisi216 – 2161L → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 2 Publications
    Mutagenesisi231 – 2311F → A: Loss of ability to bind to LF and completely nontoxic. 2 Publications
    Mutagenesisi232 – 2321L → A: Loss of ability to bind to LF and completely nontoxic. 2 Publications
    Mutagenesisi234 – 2341P → A: Loss of ability to bind to LF and completely nontoxic. 2 Publications
    Mutagenesisi236 – 2361I → A: Loss of ability to bind to LF and completely nontoxic. 2 Publications
    Mutagenesisi239 – 2391I → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 2 Publications
    Mutagenesisi255 – 2551W → A: No effect on LF-binding ability and as toxic as the wild-type. 2 Publications
    Mutagenesisi265 – 2651F → A: No effect on LF-binding ability and as toxic as the wild-type. 2 Publications
    Mutagenesisi289 – 2891P → A: Reduced toxicity in combination with lethal factor. Decreased membrane insertion and translocation of LF. 2 Publications
    Mutagenesisi342 – 3443FFD → AAA: Decrease in toxicity probably due to slow translocation of LF. 1 Publication
    Mutagenesisi342 – 3432Missing: Loss of toxicity probably due to loss of capability to translocate LF. 1 Publication
    Mutagenesisi342 – 3421F → C: Loss of toxicity probably due to loss of capability to translocate LF. 1 Publication
    Mutagenesisi344 – 3441D → A: Decrease in toxicity probably due to slow translocation of LF. 2 Publications
    Mutagenesisi375 – 3751W → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. 2 Publications
    Mutagenesisi379 – 3791M → A: No effect. 2 Publications
    Mutagenesisi381 – 3811L → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. 2 Publications
    Mutagenesisi393 – 3931I → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications
    Mutagenesisi409 – 4091T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications
    Mutagenesisi411 – 4111S → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications
    Mutagenesisi422 – 4221T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications
    Mutagenesisi426 – 4261K → A or D: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 3 Publications
    Mutagenesisi428 – 4281N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications
    Mutagenesisi440 – 4401Y → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications
    Mutagenesisi451 – 4511N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications
    Mutagenesisi454 – 4541D → A or K: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 3 Publications
    Mutagenesisi456 – 4561F → A: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 3 Publications
    Mutagenesisi512 – 5121Q → A: Loss of heptamerization capability. 2 Publications
    Mutagenesisi541 – 5411D → A: Loss of heptamerization capability. 2 Publications
    Mutagenesisi543 – 5431L → A: Decrease in heptamerization capability. 2 Publications
    Mutagenesisi581 – 5811F → A: Loss of toxicity due to defective oligomerization. 2 Publications
    Mutagenesisi583 – 5831F → A: Decrease in toxicity due to defective oligomerization. 2 Publications
    Mutagenesisi591 – 5911I → A: Loss of toxicity due to defective oligomerization. 2 Publications
    Mutagenesisi595 – 5951L → A: Loss of toxicity due to defective oligomerization. 2 Publications
    Mutagenesisi603 – 6031I → A: Loss of toxicity due to defective oligomerization. 2 Publications
    Mutagenesisi621 – 6211R → A: No effect. 2 Publications
    Mutagenesisi686 – 6861N → A: Decrease in toxicity due to decrease in cell binding. 2 Publications
    Mutagenesisi708 – 7081K → A: No effect on toxicity. 2 Publications
    Mutagenesisi709 – 7091K → A: Slight decrease in toxicity. 2 Publications
    Mutagenesisi710 – 7101Y → A: Great decrease in toxicity due to decrease in cell binding. 2 Publications
    Mutagenesisi711 – 7111N → A: Loss of toxicity due to decrease in cell binding. 2 Publications
    Mutagenesisi712 – 7121D → A: Loss of toxicity due to decrease in cell binding. 2 Publications
    Mutagenesisi713 – 7131K → A: No effect on toxicity. 2 Publications
    Mutagenesisi714 – 7141L → A: No effect on toxicity. 2 Publications
    Mutagenesisi715 – 7151P → A: Great decrease in toxicity due to decrease in cell binding. 2 Publications
    Mutagenesisi716 – 7161L → A: Decrease in toxicity due to decrease in cell binding. 2 Publications
    Mutagenesisi717 – 7171Y → A: No effect on toxicity. 2 Publications
    Mutagenesisi718 – 7181I → A: Decrease in toxicity due to decrease in cell binding. 2 Publications
    Mutagenesisi719 – 7191S → A: No effect on toxicity. 1 Publication
    Mutagenesisi720 – 7201N → A: No effect on toxicity. 2 Publications
    Mutagenesisi721 – 7211P → A: No effect on toxicity. 2 Publications
    Mutagenesisi722 – 7221N → A: No effect on toxicity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Add
    BLAST
    Chaini30 – 764735Protective antigenPRO_0000021996Add
    BLAST
    Chaini30 – 196167Protective antigen PA-20PRO_0000021997Add
    BLAST
    Chaini197 – 764568Protective antigen PA-63PRO_0000021998Add
    BLAST

    Post-translational modificationi

    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.

    Keywords - PTMi

    Cleavage on pair of basic residues

    Miscellaneous databases

    PMAP-CutDBP13423.

    Interactioni

    Subunit structurei

    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.2 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    DIPiDIP-29841N.
    IntActiP13423. 15 interactions.
    MINTiMINT-7014733.
    STRINGi261594.GBAA_pXO1_0164.

    Structurei

    Secondary structure

    1
    764
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi41 – 444
    Beta strandi47 – 559
    Beta strandi60 – 7112
    Helixi76 – 783
    Helixi84 – 863
    Beta strandi91 – 999
    Beta strandi104 – 1107
    Helixi113 – 1153
    Beta strandi116 – 1205
    Beta strandi123 – 1297
    Beta strandi135 – 1373
    Beta strandi142 – 1509
    Beta strandi155 – 1595
    Beta strandi162 – 1665
    Beta strandi168 – 1703
    Beta strandi172 – 1743
    Helixi177 – 1793
    Beta strandi186 – 1883
    Beta strandi191 – 1933
    Beta strandi199 – 2013
    Beta strandi210 – 2123
    Helixi214 – 2196
    Beta strandi221 – 2255
    Beta strandi230 – 2345
    Helixi237 – 2404
    Turni241 – 2444
    Beta strandi255 – 2584
    Beta strandi259 – 2624
    Helixi264 – 2696
    Helixi278 – 2814
    Beta strandi291 – 30212
    Beta strandi318 – 3269
    Beta strandi330 – 3323
    Beta strandi357 – 3637
    Beta strandi369 – 3713
    Helixi375 – 3795
    Beta strandi386 – 39712
    Beta strandi399 – 4013
    Beta strandi403 – 4053
    Beta strandi410 – 4145
    Turni415 – 4173
    Beta strandi418 – 4236
    Beta strandi438 – 4414
    Beta strandi448 – 4514
    Beta strandi456 – 4583
    Beta strandi461 – 4644
    Helixi465 – 47410
    Beta strandi476 – 4816
    Beta strandi487 – 4926
    Turni493 – 4964
    Beta strandi497 – 5059
    Helixi506 – 5083
    Helixi510 – 5167
    Beta strandi517 – 5226
    Turni524 – 5274
    Beta strandi530 – 5356
    Helixi542 – 5465
    Helixi552 – 5609
    Beta strandi565 – 5684
    Helixi576 – 5783
    Beta strandi579 – 5835
    Helixi585 – 59713
    Helixi603 – 6053
    Turni607 – 6093
    Beta strandi611 – 6133
    Beta strandi617 – 6226
    Beta strandi625 – 6273
    Beta strandi633 – 6364
    Helixi638 – 6447
    Beta strandi648 – 6525
    Beta strandi655 – 6584
    Helixi662 – 6665
    Beta strandi668 – 6769
    Beta strandi678 – 6803
    Beta strandi682 – 6843
    Helixi689 – 6913
    Beta strandi695 – 6973
    Turni699 – 7013
    Beta strandi703 – 7086
    Turni709 – 7135
    Beta strandi723 – 7319
    Helixi732 – 7343
    Beta strandi741 – 7433
    Beta strandi753 – 7597
    Helixi760 – 7634

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP13423.
    SMRiP13423. Positions 45-764.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13423.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 287258Domain 1, calcium-binding; LF and EF binding sitesAdd
    BLAST
    Regioni288 – 516229Domain 2, membrane insertion and heptamerizationAdd
    BLAST
    Regioni517 – 624108Domain 3, heptamerizationAdd
    BLAST
    Regioni625 – 764140Domain 4, binding to the receptorAdd
    BLAST

    Domaini

    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.1 Publication

    Sequence similaritiesi

    Belongs to the bacterial binary toxin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG284171.
    HOGENOMiHOG000034566.
    KOiK11030.
    OMAiGFNESNG.
    OrthoDBiEOG6D5FXS.

    Family and domain databases

    Gene3Di2.60.120.240. 1 hit.
    2.60.40.810. 1 hit.
    3.10.20.110. 1 hit.
    3.90.182.10. 1 hit.
    InterProiIPR003896. Bacterial_exotoxin_B.
    IPR023125. Bacterial_exotoxin_B_Fd-like.
    IPR011658. PA14.
    IPR027441. PA_dom4.
    IPR027439. PA_heptamer_dom.
    [Graphical view]
    PfamiPF03495. Binary_toxB. 1 hit.
    PF07691. PA14. 1 hit.
    [Graphical view]
    PRINTSiPR01391. BINARYTOXINB.
    SMARTiSM00758. PA14. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13423-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKRKVLIPL MALSTILVSS TGNLEVIQAE VKQENRLLNE SESSSQGLLG    50
    YYFSDLNFQA PMVVTSSTTG DLSIPSSELE NIPSENQYFQ SAIWSGFIKV 100
    KKSDEYTFAT SADNHVTMWV DDQEVINKAS NSNKIRLEKG RLYQIKIQYQ 150
    RENPTEKGLD FKLYWTDSQN KKEVISSDNL QLPELKQKSS NSRKKRSTSA 200
    GPTVPDRDND GIPDSLEVEG YTVDVKNKRT FLSPWISNIH EKKGLTKYKS 250
    SPEKWSTASD PYSDFEKVTG RIDKNVSPEA RHPLVAAYPI VHVDMENIIL 300
    SKNEDQSTQN TDSQTRTISK NTSTSRTHTS EVHGNAEVHA SFFDIGGSVS 350
    AGFSNSNSST VAIDHSLSLA GERTWAETMG LNTADTARLN ANIRYVNTGT 400
    APIYNVLPTT SLVLGKNQTL ATIKAKENQL SQILAPNNYY PSKNLAPIAL 450
    NAQDDFSSTP ITMNYNQFLE LEKTKQLRLD TDQVYGNIAT YNFENGRVRV 500
    DTGSNWSEVL PQIQETTARI IFNGKDLNLV ERRIAAVNPS DPLETTKPDM 550
    TLKEALKIAF GFNEPNGNLQ YQGKDITEFD FNFDQQTSQN IKNQLAELNA 600
    TNIYTVLDKI KLNAKMNILI RDKRFHYDRN NIAVGADESV VKEAHREVIN 650
    SSTEGLLLNI DKDIRKILSG YIVEIEDTEG LKEVINDRYD MLNISSLRQD 700
    GKTFIDFKKY NDKLPLYISN PNYKVNVYAV TKENTIINPS ENGDTSTNGI 750
    KKILIFSKKG YEIG 764
    Length:764
    Mass (Da):85,811
    Last modified:October 18, 2001 - v2
    Checksum:i3AE1EFBF48FAA03F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti314 – 3141Q → E in AAA22637. (PubMed:3148491)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti295 – 2951M → I in strain: PAI.
    Natural varianti392 – 3921N → D in strain: PAI.
    Natural varianti560 – 5601F → L in Sverdlovsk sample.
    Natural varianti565 – 5651P → S in strain: BA1024.
    Natural varianti600 – 6001A → V in strain: BA1024, V770-NP1-R, Carbosap and Ferrara.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiI39934.
    RefSeqiNP_052806.1. NC_001496.1.
    NP_652920.1. NC_003980.1.
    WP_000746486.1. NC_001496.1.
    YP_016495.2. NC_007322.2.

    Genome annotation databases

    EnsemblBacteriaiAAT28905; AAT28905; GBAA_pXO1_0164.
    GeneIDi1158723.
    2820165.
    3361714.
    KEGGibar:GBAA_pXO1_0164.
    PATRICi24662127. VBIBacAnt106580_0153.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi I39934.
    RefSeqi NP_052806.1. NC_001496.1.
    NP_652920.1. NC_003980.1.
    WP_000746486.1. NC_001496.1.
    YP_016495.2. NC_007322.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ACC X-ray 2.10 A 30-764 [» ]
    1T6B X-ray 2.50 X 30-764 [» ]
    1TX5 model - C 30-764 [» ]
    1TZN X-ray 4.30 A/B/C/D/E/F/G/H/I/J/K/L/M/O 203-764 [» ]
    1TZO X-ray 3.60 A/B/C/D/E/F/G/H/I/J/K/L/M/O 203-764 [» ]
    1V36 model - A/B/C/D/E/F/G 197-764 [» ]
    3ETB X-ray 3.80 J/K/L/M 621-764 [» ]
    3INO X-ray 1.95 A/B 624-764 [» ]
    3KWV X-ray 3.10 A/B/D/E 197-764 [» ]
    3MHZ X-ray 1.70 A 30-764 [» ]
    3Q8A X-ray 3.13 A 30-764 [» ]
    3Q8B X-ray 2.00 A 30-764 [» ]
    3Q8C X-ray 2.85 A 30-764 [» ]
    3Q8E X-ray 2.10 A 30-764 [» ]
    3Q8F X-ray 2.10 A 30-764 [» ]
    3TEW X-ray 1.45 A 30-764 [» ]
    3TEX X-ray 1.70 A 30-764 [» ]
    3TEY X-ray 2.12 A 30-764 [» ]
    3TEZ X-ray 1.83 A 30-764 [» ]
    4EE2 X-ray 1.91 A 30-764 [» ]
    4H2A X-ray 1.62 A 30-764 [» ]
    4NAM X-ray 1.70 A 30-764 [» ]
    ProteinModelPortali P13423.
    SMRi P13423. Positions 45-764.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29841N.
    IntActi P13423. 15 interactions.
    MINTi MINT-7014733.
    STRINGi 261594.GBAA_pXO1_0164.

    Chemistry

    ChEMBLi CHEMBL5352.

    Protein family/group databases

    TCDBi 1.C.42.1.1. the channel-forming bacillus anthracis protective antigen (bapa) family.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT28905 ; AAT28905 ; GBAA_pXO1_0164 .
    GeneIDi 1158723.
    2820165.
    3361714.
    KEGGi bar:GBAA_pXO1_0164.
    PATRICi 24662127. VBIBacAnt106580_0153.

    Phylogenomic databases

    eggNOGi NOG284171.
    HOGENOMi HOG000034566.
    KOi K11030.
    OMAi GFNESNG.
    OrthoDBi EOG6D5FXS.

    Enzyme and pathway databases

    BioCyci ANTHRA:GBAA_PXO1_0164-MONOMER.
    BANT261594:GJ7F-5750-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P13423.
    PMAP-CutDB P13423.

    Family and domain databases

    Gene3Di 2.60.120.240. 1 hit.
    2.60.40.810. 1 hit.
    3.10.20.110. 1 hit.
    3.90.182.10. 1 hit.
    InterProi IPR003896. Bacterial_exotoxin_B.
    IPR023125. Bacterial_exotoxin_B_Fd-like.
    IPR011658. PA14.
    IPR027441. PA_dom4.
    IPR027439. PA_heptamer_dom.
    [Graphical view ]
    Pfami PF03495. Binary_toxB. 1 hit.
    PF07691. PA14. 1 hit.
    [Graphical view ]
    PRINTSi PR01391. BINARYTOXINB.
    SMARTi SM00758. PA14. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. Cited for: REVIEW.

    Entry informationi

    Entry nameiPAG_BACAN
    AccessioniPrimary (citable) accession number: P13423
    Secondary accession number(s): Q937W2
    , Q937W3, Q9F5R7, Q9KH69, Q9RQU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In PubMed:10085028 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 PubMed:14623961 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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Plasmid, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3