位置:首页 > 蛋白库 > HLGB_STAAU
HLGB_STAAU
ID   HLGB_STAAU              Reviewed;         325 AA.
AC   P0A077; Q07226;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Gamma-hemolysin component B;
DE   AltName: Full=H-gamma-1;
DE   AltName: Full=H-gamma-I;
DE   Flags: Precursor;
GN   Name=hlgB;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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].
RX   PubMed=3075655; DOI=10.1099/00221287-134-8-2179;
RA   Cooney J.C., Mulvey M., Arbuthnott J., Foster T.;
RT   "Molecular cloning and genetic analysis of the determinant for gamma-lysin,
RT   a two-component toxin of Staphylococcus aureus.";
RL   J. Gen. Microbiol. 134:2179-2188(1988).
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. HlgB (class F) associates with either HlgA
CC       thus forming an AB toxin or with HlgC thus forming a CB toxin.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {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; AAA26639.1; -; Genomic_DNA.
DR   PIR; B49238; B49238.
DR   RefSeq; WP_000783428.1; NZ_WYDB01000001.1.
DR   PDB; 1LKF; X-ray; 1.90 A; A=27-325.
DR   PDB; 2LKF; X-ray; 2.50 A; A=27-325.
DR   PDB; 2QK7; X-ray; 2.40 A; B=27-325.
DR   PDB; 3LKF; X-ray; 1.90 A; A=27-325.
DR   PDBsum; 1LKF; -.
DR   PDBsum; 2LKF; -.
DR   PDBsum; 2QK7; -.
DR   PDBsum; 3LKF; -.
DR   AlphaFoldDB; P0A077; -.
DR   SMR; P0A077; -.
DR   TCDB; 1.C.3.4.2; the Alpha-hemolysin channel-forming toxin (Alphahl) family.
DR   ABCD; P0A077; 7 sequenced antibodies.
DR   OMA; QNAKTHT; -.
DR   EvolutionaryTrace; P0A077; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; Signal; Toxin; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..325
FT                   /note="Gamma-hemolysin component B"
FT                   /id="PRO_0000018424"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          39..53
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   TURN            54..57
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          58..69
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          72..86
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          98..114
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          120..127
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          134..142
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:3LKF"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          164..171
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          175..179
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          187..194
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   TURN            212..214
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   HELIX           229..231
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   HELIX           236..238
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   HELIX           241..244
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          251..257
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          263..282
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          287..307
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   TURN            308..311
FT                   /evidence="ECO:0007829|PDB:1LKF"
FT   STRAND          312..324
FT                   /evidence="ECO:0007829|PDB:1LKF"
SQ   SEQUENCE   325 AA;  36711 MW;  082999EB9339B6A0 CRC64;
     MKMNKLVKSS VATSMALLLL SGTANAEGKI TPVSVKKVDD KVTLYKTTAT ADSDKFKISQ
     ILTFNFIKDK SYDKDTLVLK ATGNINSGFV KPNPNDYDFS KLYWGAKYNV SISSQSNDSV
     NVVDYAPKNQ NEEFQVQNTL GYTFGGDISI SNGLSGGLNG NTAFSETINY KQESYRTTLS
     RNTNYKNVGW GVEAHKIMNN GWGPYGRDSF HPTYGNELFL AGRQSSAYAG QNFIAQHQMP
     LLSRSNFNPE FLSVLSHRQD GAKKSKITVT YQREMDLYQI RWNGFYWAGA NYKNFKTRTF
     KSTYEIDWEN HKVKLLDTKE TENNK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024