Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protective antigen

Gene

pagA

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi206Calcium1
Metal bindingi208Calcium1
Metal bindingi210Calcium1
Metal bindingi217Calcium1
Sitei712Essential for binding to cell receptor1

GO - Molecular functioni

GO - Biological processi

  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of MAPK cascade Source: UniProtKB
  • negative regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • pathogenesis Source: UniProtKB-KW
  • positive regulation of apoptotic process in other organism Source: UniProtKB
  • protein homooligomerization Source: InterPro
  • proteolysis in other organism Source: UniProtKB
  • regulation of establishment of endothelial barrier Source: UniProtKB
  • regulation of proteasomal protein catabolic process Source: UniProtKB
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.
ReactomeiR-HSA-5210891. Uptake and function of anthrax toxins.

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
Proteomesi
  • UP000000594 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi213P → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi216L → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi231F → A: Loss of ability to bind to LF and completely nontoxic. 1 Publication1
Mutagenesisi232L → A: Loss of ability to bind to LF and completely nontoxic. 1 Publication1
Mutagenesisi234P → A: Loss of ability to bind to LF and completely nontoxic. 1 Publication1
Mutagenesisi236I → A: Loss of ability to bind to LF and completely nontoxic. 1 Publication1
Mutagenesisi239I → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi255W → A: No effect on LF-binding ability and as toxic as the wild-type. 1 Publication1
Mutagenesisi265F → A: No effect on LF-binding ability and as toxic as the wild-type. 1 Publication1
Mutagenesisi289P → A: Reduced toxicity in combination with lethal factor. Decreased membrane insertion and translocation of LF. 1 Publication1
Mutagenesisi342 – 344FFD → AAA: Decrease in toxicity probably due to slow translocation of LF. 1 Publication3
Mutagenesisi342 – 343Missing : Loss of toxicity probably due to loss of capability to translocate LF. 1 Publication2
Mutagenesisi342F → C: Loss of toxicity probably due to loss of capability to translocate LF. 1 Publication1
Mutagenesisi344D → A: Decrease in toxicity probably due to slow translocation of LF. 1 Publication1
Mutagenesisi375W → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. 1 Publication1
Mutagenesisi379M → A: No effect. 1 Publication1
Mutagenesisi381L → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. 1 Publication1
Mutagenesisi393I → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi409T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi411S → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi422T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi426K → A or D: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi428N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi440Y → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi451N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi454D → A or K: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi456F → A: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi512Q → A: Loss of heptamerization capability. 1 Publication1
Mutagenesisi541D → A: Loss of heptamerization capability. 1 Publication1
Mutagenesisi543L → A: Decrease in heptamerization capability. 1 Publication1
Mutagenesisi581F → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi583F → A: Decrease in toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi591I → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi595L → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi603I → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi621R → A: No effect. 1 Publication1
Mutagenesisi686N → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi708K → A: No effect on toxicity. 1 Publication1
Mutagenesisi709K → A: Slight decrease in toxicity. 1 Publication1
Mutagenesisi710Y → A: Great decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi711N → A: Loss of toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi712D → A: Loss of toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi713K → A: No effect on toxicity. 1 Publication1
Mutagenesisi714L → A: No effect on toxicity. 1 Publication1
Mutagenesisi715P → A: Great decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi716L → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi717Y → A: No effect on toxicity. 1 Publication1
Mutagenesisi718I → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi719S → A: No effect on toxicity. 1 Publication1
Mutagenesisi720N → A: No effect on toxicity. 1 Publication1
Mutagenesisi721P → A: No effect on toxicity. 1 Publication1
Mutagenesisi722N → A: No effect on toxicity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5352.
DrugBankiDB08902. Raxibacumab.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Add BLAST29
ChainiPRO_000002199630 – 764Protective antigenAdd BLAST735
ChainiPRO_000002199730 – 196Protective antigen PA-20Add BLAST167
ChainiPRO_0000021998197 – 764Protective antigen PA-63Add BLAST568

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei196 – 197Cleavage; by furin2
Sitei343 – 344Cleavage; by chymotrypsin; required for translocation of LF and EF2

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 interactors.
MINTiMINT-7014733.

Chemistry databases

BindingDBiP13423.

Structurei

Secondary structure

1764
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi41 – 44Combined sources4
Beta strandi47 – 55Combined sources9
Beta strandi60 – 71Combined sources12
Helixi76 – 78Combined sources3
Helixi84 – 86Combined sources3
Beta strandi91 – 99Combined sources9
Beta strandi104 – 110Combined sources7
Helixi113 – 115Combined sources3
Beta strandi116 – 120Combined sources5
Beta strandi123 – 129Combined sources7
Beta strandi135 – 137Combined sources3
Beta strandi142 – 150Combined sources9
Beta strandi155 – 159Combined sources5
Beta strandi162 – 166Combined sources5
Beta strandi168 – 170Combined sources3
Beta strandi172 – 174Combined sources3
Helixi177 – 179Combined sources3
Beta strandi186 – 188Combined sources3
Beta strandi191 – 193Combined sources3
Beta strandi199 – 201Combined sources3
Beta strandi210 – 212Combined sources3
Helixi214 – 219Combined sources6
Beta strandi221 – 225Combined sources5
Beta strandi230 – 234Combined sources5
Helixi237 – 240Combined sources4
Turni241 – 244Combined sources4
Beta strandi255 – 258Combined sources4
Beta strandi259 – 262Combined sources4
Helixi264 – 269Combined sources6
Helixi278 – 281Combined sources4
Beta strandi291 – 302Combined sources12
Beta strandi318 – 326Combined sources9
Beta strandi330 – 332Combined sources3
Beta strandi357 – 363Combined sources7
Beta strandi369 – 371Combined sources3
Helixi375 – 379Combined sources5
Beta strandi386 – 397Combined sources12
Beta strandi399 – 401Combined sources3
Beta strandi403 – 405Combined sources3
Beta strandi410 – 414Combined sources5
Turni415 – 417Combined sources3
Beta strandi418 – 423Combined sources6
Beta strandi438 – 441Combined sources4
Beta strandi448 – 451Combined sources4
Beta strandi456 – 458Combined sources3
Beta strandi461 – 464Combined sources4
Helixi465 – 474Combined sources10
Beta strandi476 – 481Combined sources6
Beta strandi487 – 492Combined sources6
Turni493 – 496Combined sources4
Beta strandi497 – 505Combined sources9
Helixi506 – 508Combined sources3
Helixi510 – 516Combined sources7
Beta strandi517 – 522Combined sources6
Turni524 – 527Combined sources4
Beta strandi530 – 535Combined sources6
Helixi542 – 546Combined sources5
Helixi552 – 560Combined sources9
Beta strandi565 – 568Combined sources4
Helixi576 – 578Combined sources3
Beta strandi579 – 583Combined sources5
Helixi585 – 597Combined sources13
Helixi603 – 605Combined sources3
Turni607 – 609Combined sources3
Beta strandi611 – 613Combined sources3
Beta strandi617 – 622Combined sources6
Beta strandi625 – 627Combined sources3
Beta strandi633 – 636Combined sources4
Helixi638 – 644Combined sources7
Beta strandi648 – 652Combined sources5
Beta strandi655 – 658Combined sources4
Helixi662 – 666Combined sources5
Beta strandi668 – 676Combined sources9
Beta strandi678 – 680Combined sources3
Beta strandi682 – 684Combined sources3
Helixi689 – 691Combined sources3
Beta strandi695 – 697Combined sources3
Turni699 – 701Combined sources3
Beta strandi703 – 708Combined sources6
Turni709 – 713Combined sources5
Beta strandi723 – 731Combined sources9
Helixi732 – 734Combined sources3
Beta strandi741 – 743Combined sources3
Beta strandi753 – 759Combined sources7
Helixi760 – 763Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3J9Celectron microscopy2.90A203-764[»]
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[»]
5FR3X-ray1.94A43-764[»]
ProteinModelPortaliP13423.
SMRiP13423.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13423.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 287Domain 1, calcium-binding; LF and EF binding sitesAdd BLAST258
Regioni288 – 516Domain 2, membrane insertion and heptamerizationAdd BLAST229
Regioni517 – 624Domain 3, heptamerizationAdd BLAST108
Regioni625 – 764Domain 4, binding to the receptorAdd BLAST140

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

HOGENOMiHOG000034566.
KOiK11030.
OMAiISTNEHA.

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_dom.
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

        10         20         30         40         50
MKKRKVLIPL MALSTILVSS TGNLEVIQAE VKQENRLLNE SESSSQGLLG
60 70 80 90 100
YYFSDLNFQA PMVVTSSTTG DLSIPSSELE NIPSENQYFQ SAIWSGFIKV
110 120 130 140 150
KKSDEYTFAT SADNHVTMWV DDQEVINKAS NSNKIRLEKG RLYQIKIQYQ
160 170 180 190 200
RENPTEKGLD FKLYWTDSQN KKEVISSDNL QLPELKQKSS NSRKKRSTSA
210 220 230 240 250
GPTVPDRDND GIPDSLEVEG YTVDVKNKRT FLSPWISNIH EKKGLTKYKS
260 270 280 290 300
SPEKWSTASD PYSDFEKVTG RIDKNVSPEA RHPLVAAYPI VHVDMENIIL
310 320 330 340 350
SKNEDQSTQN TDSQTRTISK NTSTSRTHTS EVHGNAEVHA SFFDIGGSVS
360 370 380 390 400
AGFSNSNSST VAIDHSLSLA GERTWAETMG LNTADTARLN ANIRYVNTGT
410 420 430 440 450
APIYNVLPTT SLVLGKNQTL ATIKAKENQL SQILAPNNYY PSKNLAPIAL
460 470 480 490 500
NAQDDFSSTP ITMNYNQFLE LEKTKQLRLD TDQVYGNIAT YNFENGRVRV
510 520 530 540 550
DTGSNWSEVL PQIQETTARI IFNGKDLNLV ERRIAAVNPS DPLETTKPDM
560 570 580 590 600
TLKEALKIAF GFNEPNGNLQ YQGKDITEFD FNFDQQTSQN IKNQLAELNA
610 620 630 640 650
TNIYTVLDKI KLNAKMNILI RDKRFHYDRN NIAVGADESV VKEAHREVIN
660 670 680 690 700
SSTEGLLLNI DKDIRKILSG YIVEIEDTEG LKEVINDRYD MLNISSLRQD
710 720 730 740 750
GKTFIDFKKY NDKLPLYISN PNYKVNVYAV TKENTIINPS ENGDTSTNGI
760
KKILIFSKKG YEIG
Length:764
Mass (Da):85,811
Last modified:October 18, 2001 - v2
Checksum:i3AE1EFBF48FAA03F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti314Q → E in AAA22637 (PubMed:3148491).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti295M → I in strain: PAI. 1
Natural varianti392N → D in strain: PAI. 1
Natural varianti560F → L in Sverdlovsk sample. 1
Natural varianti565P → S in strain: BA1024. 1
Natural varianti600A → V in strain: BA1024, V770-NP1-R, Carbosap and Ferrara. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000746486.1. NZ_LHUO01000026.1.
WP_000746487.1. NZ_LHUN01000005.1.
WP_000746488.1. NZ_LGIF01000016.1.

Genome annotation databases

EnsemblBacteriaiAAM26109; AAM26109; BX_A0164.
AAT28905; AAT28905; GBAA_pXO1_0164.
GeneIDi3361714.
KEGGibar:GBAA_pXO1_0164.
PATRICi24662127. VBIBacAnt106580_0153.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000746486.1. NZ_LHUO01000026.1.
WP_000746487.1. NZ_LHUN01000005.1.
WP_000746488.1. NZ_LGIF01000016.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3J9Celectron microscopy2.90A203-764[»]
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[»]
5FR3X-ray1.94A43-764[»]
ProteinModelPortaliP13423.
SMRiP13423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29841N.
IntActiP13423. 15 interactors.
MINTiMINT-7014733.

Chemistry databases

BindingDBiP13423.
ChEMBLiCHEMBL5352.
DrugBankiDB08902. Raxibacumab.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM26109; AAM26109; BX_A0164.
AAT28905; AAT28905; GBAA_pXO1_0164.
GeneIDi3361714.
KEGGibar:GBAA_pXO1_0164.
PATRICi24662127. VBIBacAnt106580_0153.

Phylogenomic databases

HOGENOMiHOG000034566.
KOiK11030.
OMAiISTNEHA.

Enzyme and pathway databases

BioCyciANTHRA:GBAA_PXO1_0164-MONOMER.
ReactomeiR-HSA-5210891. Uptake and function of anthrax toxins.

Miscellaneous databases

EvolutionaryTraceiP13423.
PMAP-CutDBP13423.
PROiP13423.

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_dom.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 164 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.