ID PAG_BACAN STANDARD; PRT; 764 AA. AC P13423; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE PROTECTIVE ANTIGEN PRECURSOR (PA) [CONTAINS: PA-20; PA-63]. GN PAG. 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 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 [3] 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 AGENT WHICH INFECTS MANY MAMMALIAN SPECIES AND THAT MAY CAUSE CC DEATH. PA IS THOUGHT TO BIND TO RECEPTORS OF SENSITIVE EUKARYOTIC CC CELLS, THEREBY FACILITATING THE INTERNALIZATION OF LF OR EF. PA CC ASSOCIATED WITH LF CAUSES DEATH WHEN INJECTED, PA ASSOCIATED WITH CC EF PRODUCES EDEMA. PA INDUCES IMMUNITY TO INFECTION WITH ANTHRAX. CC -!- SUBUNIT: ANTHRAX TOXIN IS 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. ONCE ACTIVATED, PA FORMS CC HEPTAMERS WHICH INSERT INTO MEMBRANES AND FORM CATION-SELECTIVE CC 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 FURIN CLEAVES THE PROTEIN INTO TWO CC PARTS, PA-20 AND PA-63, THE LATER HEPTAMERIZE. CC -!- SIMILARITY: TO C.PERFRINGENS IOTA-B TOXIN AND TO VIP1 TOXINS IN CC BACILLUS. 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 PDB; 1ACC; 11-FEB-98. DR InterPro; IPR003896; Binary_toxB. KW Toxin; Plasmid; Calcium-binding; Signal; 3D-structure. FT SIGNAL 1 29 FT CHAIN 30 764 PROTECTIVE ANTIGEN. FT CHAIN 30 196 PA-20. FT CHAIN 197 764 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 SQ SEQUENCE 764 AA; 85811 MW; 84BB22690FEAABA5 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 TDSETRTISK 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 //