ID   SSY5_YEAS6              Reviewed;         699 AA.
AC   B5VL29;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=SPS-sensor serine protease component SSY5;
DE   AltName: Full=Endoprotease SSY5;
DE   Flags: Precursor;
GN   Name=SSY5; Synonyms=APF8; ORFNames=AWRI1631_100530;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
CC   -!- FUNCTION: Protease component of the SPS-sensor system, which regulates
CC       the expression of several amino acid-metabolizing enzymes and amino
CC       acid- and peptide-permeases in response to extracellular amino acid
CC       levels by controlling the activity of two transcription factors, STP1
CC       and STP2. Catalyzes the activation of these transcription factors,
CC       which are synthesized as latent cytoplasmic precursors, by proteolytic
CC       removal of an N-terminal inhibitory domain containing cytoplasmic
CC       retention motifs. SSY5 binds as an inactive protease complex to STP1.
CC       In response to extracellular amino acids and dependent on the other
CC       SPS-sensor components, the inhibitory propeptide is induced to
CC       dissociate, and thereby enables the catalytic domain to process STP1
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino
CC       acid sensor complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- INDUCTION: Down-regulated after extracellular amino-acid addition.
CC       {ECO:0000250}.
CC   -!- PTM: The propeptide is autoproteolytically cleaved from the catalytic
CC       domain but remains associated, forming an inactive protease complex.
CC       This processing occurs even in the absence of signaling (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S64 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDZ71365.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; ABSV01001268; EDZ71365.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; B5VL29; -.
DR   MEROPS; S64.001; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR012985; Peptidase_S64_Ssy5.
DR   Pfam; PF08192; Peptidase_S64; 1.
DR   PIRSF; PIRSF011716; Peptidase_S64_Ssy5; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Zymogen.
FT   PROPEP          1..381
FT                   /id="PRO_0000377375"
FT   CHAIN           382..699
FT                   /note="SPS-sensor serine protease component SSY5"
FT                   /id="PRO_0000377376"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..699
FT                   /note="Serine protease"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        465
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        545
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        640
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   699 AA;  77602 MW;  22F7245938170E29 CRC64;
     MVRFFGLNKE KNEEKENTDL PADNEQNAAE TSSSNVSGNE ERIDPNSRDT NPENANNDDA
     STTFGSSIQS SSIFSRGRMT YGTGASSSMA TSEMRSHSSG HSRSKNSKNL QGFKDVGKPL
     RAVSFLNPVK EEESQDTQNT LDVSSSTSST LATSGNAREN SFTSRRSITL EYIHKSLSEL
     EENLVDIMDD IHQDVISISK AVIEAIEYFK EFLPTTRDRI PYRISLEKSS SLRKINKIVL
     HFLDNLLVSD AFSNSRSILL RRFYFFLKKL NLITDDDLIS ESGVLPCLSV FCIGSHCNLP
     SMDKLGMILD ELTKMDSSII SDQEGAFIAP ILRGITPKSS ILTIMFGLPN LQHEHYEMIK
     VLYSLFPDVH MYCVKDYIKK AASAVGSIPS HTAATIDTIA PTKFQFSPPY AVSENPLELP
     ISMSLSTETS AKITGTLGGY LFPQTGSDEK FSQFASCSFA ITCAHVVLSE KQDYPNVMVP
     SNVLQTSYKK VLTKESDRYP DGSVEKTAFL EEVQRIDQNL NWQKSNKFGQ VVWGERAIVD
     HRLSDFAIIK VNSSFKCQNT LGNGLKSFPD PTLRFQNLHV KRKIFKMKPG MKVFKIGAST
     GYTSGELNST KLVYWADGKL QSSEFVVASP TPLFASAGDS GAWILTKLED RLGLGLVGML
     HSYDGEQRQF GLFTPIGDIL ERLHAVTKIQ WDIDPQLDG