HLY1C_STACC
ID HLY1C_STACC Reviewed; 43 AA.
AC P85219;
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 H1C;
OS Staphylococcus cohnii subsp. cohnii.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=74704;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND FORMYLATION AT MET-1.
RC STRAIN=ZMF 77 {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 from sheep
CC (HD(50)=7.53 mM), rabbit (HD(50)=28.07 mM), guinea pig (HD(50)=4.23
CC mM), dog (HD(50)=4.37 mM) and human (HD(50)=3.32 mM). 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 RefSeq; WP_019469819.1; NZ_PPQC01000014.1.
DR AlphaFoldDB; P85219; -.
DR SMR; P85219; -.
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 H1C"
FT /id="PRO_0000302131"
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