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};
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; 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