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HLGA_STAAM
ID   HLGA_STAAM              Reviewed;         309 AA.
AC   P0A071; P31714; Q07225; Q53689; Q53690;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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; OrderedLocusNames=SAV2419;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- FUNCTION: Toxin that seems to act by forming pores in the membrane of
CC       the cell. Has a hemolytic and a leucotoxic activity (By similarity).
CC       {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P0A071; A0A0H3JX61: hlgB; NbExp=2; IntAct=EBI-16223478, EBI-16223472;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB58581.1; -; Genomic_DNA.
DR   RefSeq; WP_000594519.1; NC_002758.2.
DR   PDB; 3B07; X-ray; 2.50 A; B/D/F/H=30-309.
DR   PDB; 4P1Y; X-ray; 2.99 A; B/D/F/H=42-309.
DR   PDBsum; 3B07; -.
DR   PDBsum; 4P1Y; -.
DR   AlphaFoldDB; P0A071; -.
DR   SMR; P0A071; -.
DR   DIP; DIP-59713N; -.
DR   IntAct; P0A071; 1.
DR   PaxDb; P0A071; -.
DR   EnsemblBacteria; BAB58581; BAB58581; SAV2419.
DR   KEGG; sav:SAV2419; -.
DR   HOGENOM; CLU_075311_0_0_9; -.
DR   OMA; ANPFTEI; -.
DR   PhylomeDB; P0A071; -.
DR   BioCyc; SAUR158878:SAV_RS13185-MON; -.
DR   Proteomes; UP000002481; Chromosome.
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; Hemolysis; Secreted; Signal; Toxin; Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..309
FT                   /note="Gamma-hemolysin component A"
FT                   /id="PRO_0000018419"
FT   STRAND          42..51
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   TURN            52..55
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          56..65
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          70..84
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          98..113
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          118..125
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          131..147
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          151..179
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          182..189
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   TURN            204..207
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          212..215
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   HELIX           216..219
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   HELIX           228..231
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          237..244
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          246..248
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          250..270
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          273..295
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   TURN            296..299
FT                   /evidence="ECO:0007829|PDB:3B07"
FT   STRAND          300..307
FT                   /evidence="ECO:0007829|PDB:3B07"
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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