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Database: UniProt
Entry: A0A0X3USA5_9ACTN
LinkDB: A0A0X3USA5_9ACTN
Original site: A0A0X3USA5_9ACTN 
ID   A0A0X3USA5_9ACTN        Unreviewed;       384 AA.
AC   A0A0X3USA5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:KUL35448.1};
GN   ORFNames=ADL12_19860 {ECO:0000313|EMBL:KUL35448.1};
OS   Streptomyces regalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL35448.1, ECO:0000313|Proteomes:UP000053923};
RN   [1] {ECO:0000313|Proteomes:UP000053923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUL35448.1}.
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DR   EMBL; LLZG01000153; KUL35448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X3USA5; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000053923; Unassembled WGS sequence.
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   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KUL35448.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053923};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..384
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038661811"
FT   TRANSMEM        353..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..309
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          321..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  39112 MW;  9D3C2F468963A469 CRC64;
     MAGRTTSGPM LATRAGAVAA ALALAVVAAG TAAPADSGAL RESEWALTAL KAEQAWEITR
     GEGVTVAVIG TGVDASHPDL AGRVVKSRDV DGTRDEGGGS AAIQGTHAAG VIAGTGRNFD
     GDGLFGLAPK ARILPFSVYR DNTALTAATA RSIMDAARQG AEVIDVTVGF PRPSDDLKTA
     IEFATDRDAL VVAGAGDTGG TGNAETYPAA YPGVLSVTAM DKKGAIWPDS HHGKDVDLAA
     PGVDILTTAR NRDYWTGSGT AFAASWVAGS AALLRSEHPK WTVSQVTRTL TETATQQGKA
     DWDSRYGRGV VAPAAALSQR AVPSGSEAAA PPKDQAANAE NHATSEPSDA GPALIVLAVT
     TTLLVLAVIA WLLIRRSVTP TDND
//
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