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Database: UniProt
Entry: G8WXP1_STREN
LinkDB: G8WXP1_STREN
Original site: G8WXP1_STREN 
ID   G8WXP1_STREN            Unreviewed;       336 AA.
AC   G8WXP1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Secreted serine protease {ECO:0000313|EMBL:AEW96871.1};
GN   OrderedLocusNames=SCATT_45000 {ECO:0000313|EMBL:AEW96871.1};
OS   Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS   / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptantibioticus.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW96871.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; CP003219; AEW96871.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8WXP1; -.
DR   STRING; 1003195.SCATT_45000; -.
DR   KEGG; scy:SCATT_45000; -.
DR   PATRIC; fig|1003195.29.peg.4493; -.
DR   eggNOG; ENOG5030I4K; Bacteria.
DR   HOGENOM; CLU_011263_13_3_11; -.
DR   Proteomes; UP000007842; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AEW96871.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:AEW96871.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007842};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        308..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..248
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   336 AA;  33488 MW;  F0163C26A186CDF3 CRC64;
     MTELVGQVLP GKDYTSPTGN GWNDTDGHGT SMAMLIAGTG DDGGIVGLAP GAKILPLRVL
     AGGGPNRPGR DLKRVADAIH YAADHGAKVI NIAIGVPDLS SSPEDRAPLG PAVQYALKRG
     SLVFAATGND AQSGNPLSYP AATPGAVGVG AVDKTGTVGK FSTYGPQVAL VAPGVDVPGH
     CSKSLAHYGD GYCIGYGTSE ATALASASAA LVWAKHPDWT NNQVLRVLIN TAGKPKTGKI
     PSEYIGYGTV RPRVALLDGA GDPGPADVNP LFPNLGSPSP STAPAGKSSG KPTQAGAARG
     GGAGDTGAWM WAGIAAAVVV VGGGLGAAVL RRRRAH
//
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