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P13423

- PAG_BACAN

UniProt

P13423 - PAG_BACAN

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Protein
Protective antigen
Gene
pagA, pag, pXO1-110, BXA0164, GBAA_pXO1_0164
Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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. 2 Publications
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 – 2929
Add
BLAST
Chaini30 – 764735Protective antigen
PRO_0000021996Add
BLAST
Chaini30 – 196167Protective antigen PA-20
PRO_0000021997Add
BLAST
Chaini197 – 764568Protective antigen PA-63
PRO_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.

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

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.

Miscellaneous databases

EvolutionaryTraceiP13423.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 287258Domain 1, calcium-binding; LF and EF binding sites
Add
BLAST
Regioni288 – 516229Domain 2, membrane insertion and heptamerization
Add
BLAST
Regioni517 – 624108Domain 3, heptamerization
Add
BLAST
Regioni625 – 764140Domain 4, binding to the receptor
Add
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.2 Publications

Sequence similaritiesi

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti314 – 3141Q → E in AAA22637. 1 Publication

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

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  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: September 3, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In 1 Publication 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 1 Publication 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

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