ID   PSMA1_STAAW             Reviewed;          21 AA.
AC   A9JX05;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Phenol-soluble modulin alpha 1 peptide;
GN   Name=psmA1; OrderedLocusNames=MW0406.4;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, FORMYLATION AT MET-1, FUNCTION AS A VIRULENCE
RP   FACTOR, IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY AGR.
RX   PubMed=17994102; DOI=10.1038/nm1656;
RA   Wang R., Braughton K.R., Kretschmer D., Bach T.-H.L., Queck S.Y., Li M.,
RA   Kennedy A.D., Dorward D.W., Klebanoff S.J., Peschel A., DeLeo F.R.,
RA   Otto M.;
RT   "Identification of novel cytolytic peptides as key virulence determinants
RT   for community-associated MRSA.";
RL   Nat. Med. 13:1510-1514(2007).
CC   -!- FUNCTION: Peptide which can recruit, activate and subsequently lyse
CC       human neutrophils, thus eliminating the main cellular defense against
CC       infection. Stimulates the secretion of the chemotactic factor
CC       interleukin-8 (IL-8). The ensuing activation process triggers an
CC       inflammatory response in the host, thus contributing greatly to
CC       virulence. Also possesses hemolytic activity, which may contribute to
CC       the development of disease. {ECO:0000269|PubMed:17994102}.
CC   -!- INDUCTION: Up-regulated by agr. {ECO:0000269|PubMed:17994102}.
CC   -!- MISCELLANEOUS: Peptide production is higher in most prevalent
CC       community-associated MRSA strains than in hospital-associated MRSA
CC       strains.
CC   -!- SIMILARITY: Belongs to the phenol-soluble modulin alpha peptides
CC       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; BA000033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006301; DAA06122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JX05; -.
DR   SMR; A9JX05; -.
DR   PHI-base; PHI:4599; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR031429; PSM_alpha.
DR   Pfam; PF17063; PSMalpha; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Formylation; Virulence.
FT   PEPTIDE         1..21
FT                   /note="Phenol-soluble modulin alpha 1 peptide"
FT                   /id="PRO_0000345042"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:17994102"
SQ   SEQUENCE   21 AA;  2260 MW;  F291499952C7572D CRC64;
     MGIIAGIIKV IKSLIEQFTG K