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HLGA_STAAU
ID   HLGA_STAAU              Reviewed;         309 AA.
AC   P0A074; P31714; Q07225; Q53689; Q53690;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Gamma-hemolysin component A;
DE   AltName: Full=H-gamma-2;
DE   AltName: Full=H-gamma-II;
DE   Flags: Precursor;
GN   Name=hlgA; Synonyms=hlg2;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Smith 5R;
RX   PubMed=8423103; DOI=10.1128/iai.61.2.768-771.1993;
RA   Cooney J.C., Kienle Z., Foster T.J., O'Toole P.W.;
RT   "The gamma-hemolysin locus of Staphylococcus aureus comprises three linked
RT   genes, two of which are identical to the genes for the F and S components
RT   of leukocidin.";
RL   Infect. Immun. 61:768-771(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MRSA NO. 4;
RX   PubMed=7763998; DOI=10.1271/bbb.57.1234;
RA   Rahman A., Izaki K., Kamio Y.;
RT   "Gamma-hemolysin genes in the same family with lukF and lukS genes in
RT   methicillin resistant Staphylococcus aureus.";
RL   Biosci. Biotechnol. Biochem. 57:1234-1236(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31890 / P83;
RX   PubMed=8520122; DOI=10.1271/bbb.59.1786;
RA   Sudo K., Choorit W., Asami I., Kaneko J., Muramoto K., Kamio Y.;
RT   "Substitution of lysine for arginine in the N-terminal 217th amino acid
RT   residue of the H gamma II of Staphylococcal gamma-hemolysin lowers the
RT   activity of the toxin.";
RL   Biosci. Biotechnol. Biochem. 59:1786-1789(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-44.
RC   STRAIN=ATCC 49775 / V8;
RX   PubMed=7558328; DOI=10.1128/iai.63.10.4121-4129.1995;
RA   Prevost G., Cribier B., Couppie P., Petiau P., Supersac G.,
RA   Finck-Barbancon V., Monteil H., Piemont Y.;
RT   "Panton-Valentine leucocidin and gamma-hemolysin from Staphylococcus aureus
RT   ATCC 49775 are encoded by distinct genetic loci and have different
RT   biological activities.";
RL   Infect. Immun. 63:4121-4129(1995).
RN   [5]
RP   PROTEIN SEQUENCE OF 30-87 AND 305-309.
RC   STRAIN=RIMD 310925;
RX   PubMed=8467905; DOI=10.1016/0014-5793(93)80611-w;
RA   Kamio Y., Rahman A., Nariya H., Ozawa T., Izaki K.;
RT   "The two Staphylococcal bi-component toxins, leukocidin and gamma-
RT   hemolysin, share one component in common.";
RL   FEBS Lett. 321:15-18(1993).
RN   [6]
RP   TOXIC ACTIVITY.
RC   STRAIN=ATCC 49775 / V8;
RX   PubMed=9804914; DOI=10.1016/s0005-2736(98)00160-6;
RA   Ferreras M., Hoeper F., Dalla Serra M., Colin D.A., Prevost G.,
RA   Menestrina G.;
RT   "The interaction of Staphylococcus aureus bi-component gamma-hemolysins and
RT   leucocidins with cells and lipid membranes.";
RL   Biochim. Biophys. Acta 1414:108-126(1998).
CC   -!- FUNCTION: Toxin that seems to act by forming pores in the membrane of
CC       the cell. Has a hemolytic and a leucotoxic activity.
CC   -!- SUBUNIT: Toxicity requires sequential binding and synergistic
CC       association of a class S and a class F component which form
CC       heterooligomeric complexes. HlgA (class S) associates with HlgB (class
CC       F) thus forming an AB toxin in strains producing both gamma-hemolysins
CC       and leukocidins. HlgA and LukF-PV can also form a complex.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA57276.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L01055; AAA26637.1; -; Genomic_DNA.
DR   EMBL; S65052; AAC60444.1; -; Genomic_DNA.
DR   EMBL; D42143; BAA07714.1; -; Genomic_DNA.
DR   EMBL; X81586; CAA57276.1; ALT_INIT; Genomic_DNA.
DR   PIR; JC4282; JC4282.
DR   PIR; S49271; S49271.
DR   RefSeq; WP_000594519.1; NZ_WYDB01000001.1.
DR   PDB; 2QK7; X-ray; 2.40 A; A=30-309.
DR   PDBsum; 2QK7; -.
DR   AlphaFoldDB; P0A074; -.
DR   SMR; P0A074; -.
DR   TCDB; 1.C.3.4.2; the Alpha-hemolysin channel-forming toxin (Alphahl) family.
DR   OMA; ANPFTEI; -.
DR   EvolutionaryTrace; P0A074; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR003963; Bi-component_toxin_staph.
DR   InterPro; IPR016183; Leukocidin/Hemolysin_toxin.
DR   InterPro; IPR036435; Leukocidin/porin_MspA_sf.
DR   Pfam; PF07968; Leukocidin; 1.
DR   PRINTS; PR01468; BICOMPNTOXIN.
DR   SUPFAM; SSF56959; SSF56959; 1.
DR   TIGRFAMs; TIGR01002; hlyII; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytolysis; Direct protein sequencing; Hemolysis; Secreted;
KW   Signal; Toxin; Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:7558328,
FT                   ECO:0000269|PubMed:8467905"
FT   CHAIN           30..309
FT                   /note="Gamma-hemolysin component A"
FT                   /id="PRO_0000018422"
FT   VARIANT         246
FT                   /note="R -> K (in strain: ATCC 49775 and ATCC 31890; loss
FT                   of 40-50% of hemolytic activity in ATCC 31890)"
FT   CONFLICT        45
FT                   /note="R -> H (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="R -> H (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="V -> G (in Ref. 4; CAA57276)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="H -> P (in Ref. 4; CAA57276)"
FT                   /evidence="ECO:0000305"
FT   STRAND          41..51
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   TURN            52..55
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          56..66
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          71..84
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          99..112
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          132..141
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          145..150
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          159..167
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          171..178
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          180..189
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   TURN            204..207
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          212..215
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   HELIX           216..219
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   HELIX           228..231
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          238..245
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          250..269
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          274..295
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   TURN            296..299
FT                   /evidence="ECO:0007829|PDB:2QK7"
FT   STRAND          300..307
FT                   /evidence="ECO:0007829|PDB:2QK7"
SQ   SEQUENCE   309 AA;  34956 MW;  15CAE12E1025B616 CRC64;
     MIKNKILTAT LAVGLIAPLA NPFIEISKAE NKIEDIGQGA EIIKRTQDIT SKRLAITQNI
     QFDFVKDKKY NKDALVVKMQ GFISSRTTYS DLKKYPYIKR MIWPFQYNIS LKTKDSNVDL
     INYLPKNKID SADVSQKLGY NIGGNFQSAP SIGGSGSFNY SKTISYNQKN YVTEVESQNS
     KGVKWGVKAN SFVTPNGQVS AYDQYLFAQD PTGPAARDYF VPDNQLPPLI QSGFNPSFIT
     TLSHERGKGD KSEFEITYGR NMDATYAYVT RHRLAVDRKH DAFKNRNVTV KYEVNWKTHE
     VKIKSITPK
 
 
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