SSY5_YEAS7
ID SSY5_YEAS7 Reviewed; 699 AA.
AC A6ZQH6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=SPS-sensor serine protease component SSY5;
DE AltName: Full=Endoprotease SSY5;
DE Flags: Precursor;
GN Name=SSY5; Synonyms=APF8; ORFNames=SCY_3137;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 ---------------------------------------------------------------------------
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; AAFW02000044; EDN63228.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZQH6; -.
DR MEROPS; S64.001; -.
DR EnsemblFungi; EDN63228; EDN63228; SCY_3137.
DR HOGENOM; CLU_012881_1_0_1; -.
DR Proteomes; UP000007060; 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_0000377377"
FT CHAIN 382..699
FT /note="SPS-sensor serine protease component SSY5"
FT /id="PRO_0000377378"
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; 77452 MW; 8EDE9BB5AFE270BE CRC64;
MVRFFGLNKK KNEEKENTDL PADNEQNAAE TSSSNVSGNE ERIDPNSHDA NPENANNDDA
STTFGSSIQS SSIFSRGRMT YGTGASSSMA TSEMRSHSSG HSGSKNSKNL 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 LFPQTGSDKK 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