ID PAG_BACAN STANDARD; PRT; 764 AA. AC P13423; Q9RQU2; Q9F5R7; Q9KH69; DT 01-JAN-1990 (Rel. 13, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 01-MAR-2002 (Rel. 41, Last annotation update) DE Protective antigen precursor (PA) (PA-83) (PA83) (Anthrax toxins DE translocating protein) [Contains: PA-20 (PA20); PA-63 (PA63)]. GN PAGA OR PAG OR PXO1-110. OS Bacillus anthracis. OG Plasmid pXO1. OC Bacteria; Firmicutes; Bacillus/Clostridium group; OC Bacillus/Staphylococcus group; Bacillus. OX NCBI_TaxID=1392; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89172073; PubMed=3148491; RA Welkos S.L., Lowe J.R., Eden-Mccutchan F., Vodkin M., Leppla S.H., RA Schmidt J.J.; RT "Sequence and analysis of the DNA encoding protective antigen of RT Bacillus anthracis."; RL Gene 69:287-300(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=28, 33, BA1024, AND BA1035; RX MEDLINE=99214082; PubMed=10197996; RA Price L.B., Hugh-Jones M., Jackson P.J., Keim P.; RT "Genetic diversity in the protective antigen gene of Bacillus RT anthracis."; RL J. Bacteriol. 181:2358-2362(1999). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=V770-NP1-R / ATCC 14185; RX MEDLINE=20359347; PubMed=10899854; RA Cohen S., Mendelson I., Altboum Z., Kobiler D., Elhanany E., Bino T., RA Leitner M., Inbar I., Rosenberg H., Gozes Y., Barak R., Fisher M., RA Kronman C., Velan B., Shafferman A.; RT "Attenuated nontoxinogenic and nonencapsulated recombinant Bacillus RT anthracis spore vaccines protect against anthrax."; RL Infect. Immun. 68:4549-4558(2000). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Sterne; RX MEDLINE=99445483; PubMed=10515943; RA Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., RA Keim P., Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., RA Martinez Y., Ricke D., Svensson R., Jackson P.J.; RT "Sequence and organization of pXO1, the large Bacillus anthracis RT plasmid harboring the Anthrax toxin genes."; RL J. Bacteriol. 181:6509-6515(1999). RN [5] RP DOMAINS. RX MEDLINE=91332080; PubMed=1651334; RA Singh Y., Klimpel K.R., Quinn C.P., Chaudhary V.K., Leppla S.H.; RT "The carboxyl-terminal end of protective antigen is required for RT receptor binding and anthrax toxin activity."; RL J. Biol. Chem. 266:15493-15497(1991). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX MEDLINE=97192099; PubMed=9039918; RA Petosa C., Collier R.J., Klimpel K.R., Leppla S.H., Liddington R.C.; RT "Crystal structure of the anthrax toxin protective antigen."; RL Nature 385:833-838(1997). CC -!- FUNCTION: One of the three proteins composing the anthrax toxin, CC the agent which infects many mammalian species and that may cause CC death. PA binds to a receptor (ATR) in sensitive eukaryotic CC cells, thereby facilitating the translocation of the enzymatic CC toxin components, edema factor and lethal factor, across the CC target cell membrane. PA associated with LF causes death when CC injected, PA associated with EF produces edema. PA induces CC immunity to infection with anthrax. CC -!- SUBUNIT: Anthrax toxins are composed of three distinct proteins, a CC protective antigen (PA), a lethal factor (LF) and an edema factor CC (EF). None of these is toxic by itself. PA+LF forms the lethal CC toxin (LeTx); PA+EF forms the edema toxin (EdTx). Once activated, CC PA forms heptamers which insert into membranes and form cation- CC selective channels. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- DOMAIN: THE C-TERMINAL PART OF PA IS REQUIRED FOR RECEPTOR BINDING CC AND TOXIC ACTIVITY. CC -!- PTM: Proteolytic activation by a furin-like protease cleaves the CC protein into two parts, PA-20 and PA-63, the later heptamerize. CC -!- SIMILARITY: BELONGS TO THE BACTERIAL BINARY TOXIN FAMILY. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M22589; AAA22637.1; -. DR EMBL; AF306778; AAG24446.1; -. DR EMBL; AF306779; AAG24447.1; -. DR EMBL; AF306780; AAG24448.1; -. DR EMBL; AF306781; AAG24449.1; -. DR EMBL; AF306782; AAG24450.1; -. DR EMBL; AF306783; AAG24451.1; -. DR EMBL; AF268967; AAF86457.1; -. DR EMBL; AF065404; AAD32414.1; -. DR PDB; 1ACC; 11-FEB-98. DR InterPro; IPR003896; Binary_toxB. DR PRINTS; PR01391; BINARYTOXINB. KW Toxin; Virulence; Calcium-binding; Signal; Plasmid; 3D-structure. FT SIGNAL 1 29 FT CHAIN 30 764 PROTECTIVE ANTIGEN. FT CHAIN 30 196 PROTECTIVE ANTIGEN, PA-20. FT CHAIN 197 764 PROTECTIVE ANTIGEN, PA-63. FT DOMAIN 30 287 DOMAIN 1, CALCIUM-BINDING. FT DOMAIN 288 516 DOMAIN 2, HEPTAMERIZATION. FT DOMAIN 517 764 DOMAIN 3. FT CA_BIND 206 206 FT CA_BIND 208 208 FT CA_BIND 210 210 FT CA_BIND 217 217 FT VARIANT 560 560 F -> L (IN SVERDLOVSK SAMPLE). FT VARIANT 565 565 P -> S (IN STRAIN BA1024). FT VARIANT 600 600 A -> V (IN STRAINS BA1024 AND V770-NP1- FT R). FT CONFLICT 314 314 Q -> E (IN REF. 1). SQ SEQUENCE 764 AA; 85810 MW; 3AE1EFBF48FAA03F CRC64; MKKRKVLIPL MALSTILVSS TGNLEVIQAE VKQENRLLNE SESSSQGLLG YYFSDLNFQA PMVVTSSTTG DLSIPSSELE NIPSENQYFQ SAIWSGFIKV KKSDEYTFAT SADNHVTMWV DDQEVINKAS NSNKIRLEKG RLYQIKIQYQ RENPTEKGLD FKLYWTDSQN KKEVISSDNL QLPELKQKSS NSRKKRSTSA GPTVPDRDND GIPDSLEVEG YTVDVKNKRT FLSPWISNIH EKKGLTKYKS SPEKWSTASD PYSDFEKVTG RIDKNVSPEA RHPLVAAYPI VHVDMENIIL SKNEDQSTQN TDSQTRTISK NTSTSRTHTS EVHGNAEVHA SFFDIGGSVS AGFSNSNSST VAIDHSLSLA GERTWAETMG LNTADTARLN ANIRYVNTGT APIYNVLPTT SLVLGKNQTL ATIKAKENQL SQILAPNNYY PSKNLAPIAL NAQDDFSSTP ITMNYNQFLE LEKTKQLRLD TDQVYGNIAT YNFENGRVRV DTGSNWSEVL PQIQETTARI IFNGKDLNLV ERRIAAVNPS DPLETTKPDM TLKEALKIAF GFNEPNGNLQ YQGKDITEFD FNFDQQTSQN IKNQLAELNA TNIYTVLDKI KLNAKMNILI RDKRFHYDRN NIAVGADESV VKEAHREVIN SSTEGLLLNI DKDIRKILSG YIVEIEDTEG LKEVINDRYD MLNISSLRQD GKTFIDFKKY NDKLPLYISN PNYKVNVYAV TKENTIINPS ENGDTSTNGI KKILIFSKKG YEIG //