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HLGA_STAAC
ID   HLGA_STAAC              Reviewed;         309 AA.
AC   Q5HDD6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
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; OrderedLocusNames=SACOL2419;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW37243.1; -; Genomic_DNA.
DR   RefSeq; WP_000594519.1; NC_002951.2.
DR   AlphaFoldDB; Q5HDD6; -.
DR   SMR; Q5HDD6; -.
DR   EnsemblBacteria; AAW37243; AAW37243; SACOL2419.
DR   KEGG; sac:SACOL2419; -.
DR   HOGENOM; CLU_075311_0_0_9; -.
DR   OMA; ANPFTEI; -.
DR   Proteomes; UP000000530; 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   3: Inferred from homology;
KW   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_0000045214"
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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