ID   HBLA_BACCE              Reviewed;         375 AA.
AC   P80172;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Hemolysin BL-binding component;
DE   AltName: Full=Enterotoxin 40 kDa subunit;
DE   Flags: Precursor;
GN   Name=hblA;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 32-47.
RC   STRAIN=F837/76;
RX   PubMed=7693651; DOI=10.1128/jb.175.21.6760-6766.1993;
RA   Heinrichs J.H., Beecher D.J., Macmillan J.D., Zilinskas B.A.;
RT   "Molecular cloning and characterization of the hblA gene encoding the B
RT   component of hemolysin BL from Bacillus cereus.";
RL   J. Bacteriol. 175:6760-6766(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 34-48.
RC   STRAIN=1230-88;
RX   PubMed=8319899; DOI=10.1111/j.1574-6968.1993.tb06301.x;
RA   Granum P.E., Nissen H.;
RT   "Sphingomyelinase is part of the 'enterotoxin complex' produced by Bacillus
RT   cereus.";
RL   FEMS Microbiol. Lett. 110:97-100(1993).
CC   -!- FUNCTION: Cytotoxic protein, part of the enterotoxin complex.
CC       Responsible for binding to erythrocytes. This enterotoxin is thought to
CC       be the cause of the diarrheal form of gastroenteritis caused by food-
CC       borne strains of B.cereus.
CC   -!- SUBUNIT: Composed of a binding component, B, and two lytic components,
CC       L1 and L2. All three subunits act synergically to cause hemolysis.
CC   -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
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DR   EMBL; L20441; AAA22522.1; -; Genomic_DNA.
DR   PIR; A49336; A49336.
DR   PDB; 2NRJ; X-ray; 2.03 A; A=32-375.
DR   PDBsum; 2NRJ; -.
DR   AlphaFoldDB; P80172; -.
DR   SMR; P80172; -.
DR   EvolutionaryTrace; P80172; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR008414; HBL.
DR   Pfam; PF05791; Bacillus_HBL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytolysis; Direct protein sequencing; Enterotoxin; Hemolysis;
KW   Host cell membrane; Host membrane; Membrane; Secreted; Signal; Toxin;
KW   Transmembrane; Transmembrane helix; Virulence.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:7693651"
FT   CHAIN           32..375
FT                   /note="Hemolysin BL-binding component"
FT                   /id="PRO_0000021398"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TURN            33..36
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           48..74
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           91..111
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           113..144
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           147..202
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           207..217
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   STRAND          239..244
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   TURN            245..247
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           257..268
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           273..326
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   TURN            332..335
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           336..338
FT                   /evidence="ECO:0007829|PDB:2NRJ"
FT   HELIX           339..364
FT                   /evidence="ECO:0007829|PDB:2NRJ"
SQ   SEQUENCE   375 AA;  41567 MW;  8D65F9DB92C7CE28 CRC64;
     MIKKIPYKLL AVSTLLTITT ANVVSPVATF ASEIEQTNNG DTALSANEAK MKETLQKAGL
     FAKSMNAYSY MLIKNPDVNF EGITINGYVD LPGRIVQDQK NARAHAVTWD TKVKKQLLDT
     LTGIVEYDTT FDNYYETMVE AINTGDGETL KEGITDLRGE IQQNQKYAQQ LIEELTKLRD
     SIGHDVRAFG SNKELLQSIL KNQGADVDAD QKRLEEVLGS VNYYKQLESD GFNVMKGAIL
     GLPIIGGIIV GVARDNLGKL EPLLAELRQT VDYKVTLNRV VGVAYSNINE IDKALDDAIN
     ALTYMSTQWH DLDSQYSGVL GHIENAAQKA DQNKFKFLKP NLNAAKDSWK TLRTDAVTLK
     EGIKELKVET VTPQK