ID   HLY1U_STAUR             Reviewed;          43 AA.
AC   P85222;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Hemolysin H1U;
OS   Staphylococcus ureilyticus (Staphylococcus cohnii subsp. urealyticus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=94138;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND FORMYLATION AT MET-1.
RC   STRAIN=ZMF 535 {ECO:0000269|PubMed:18752624};
RX   PubMed=18752624; DOI=10.1111/j.1574-6968.2008.01321.x;
RA   Mak P., Maszewska A., Rozalska M.;
RT   "The amino acid sequences and activities of synergistic hemolysins from
RT   Staphylococcus cohnii.";
RL   FEMS Microbiol. Lett. 287:230-235(2008).
CC   -!- FUNCTION: Virulence factor. Causes hemolysis of erythrocytes. Acts
CC       synergistically with beta-hemolysins from S.aureus ATCC 25923.
CC       Cytotoxic towards human dermal fibroblasts.
CC       {ECO:0000269|PubMed:18752624}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18752624}.
CC   -!- SIMILARITY: Belongs to the staphylococcal hemolytic protein family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P85222; -.
DR   SMR; P85222; -.
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; IPR008846; PSMbeta.
DR   Pfam; PF05480; PSMbeta; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Formylation; Hemolysis; Secreted;
KW   Toxin; Virulence.
FT   PEPTIDE         1..43
FT                   /note="Hemolysin H1U"
FT                   /id="PRO_0000302133"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:18752624"
SQ   SEQUENCE   43 AA;  4429 MW;  2FE5DF5B9E357FB3 CRC64;
     MSGIVEAISN AVKSGLDHDW VNMGTSIADV VAKGADFIAG FFS