ID   A0A117IVB3_9ACTN        Unreviewed;       405 AA.
AC   A0A117IVB3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Type VII secretion-associated serine protease mycosin {ECO:0000313|EMBL:KUH36935.1};
GN   ORFNames=ATE80_20990 {ECO:0000313|EMBL:KUH36935.1};
OS   Streptomyces kanasensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH36935.1, ECO:0000313|Proteomes:UP000054011};
RN   [1] {ECO:0000313|EMBL:KUH36935.1, ECO:0000313|Proteomes:UP000054011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZX01 {ECO:0000313|EMBL:KUH36935.1,
RC   ECO:0000313|Proteomes:UP000054011};
RA   Zhang G., Han L., Feng J., Zhang X.;
RT   "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT   kanasensis ZX01.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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:KUH36935.1}.
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DR   EMBL; LNSV01000060; KUH36935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117IVB3; -.
DR   STRING; 936756.ATE80_20990; -.
DR   Proteomes; UP000054011; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR023834; T7SS_pept_S8A_mycosin.
DR   NCBIfam; TIGR03921; T7SS_mycosin; 1.
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.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054011};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..405
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007149020"
FT   TRANSMEM        369..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          56..321
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          88..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        114
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        274
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   405 AA;  41605 MW;  D989C056D17FE11C CRC64;
     MVTATAAAAL TVLCLPAGPA SADTPGQCTF PAEPYEGRPW ALQRVLLDEV WKQSTGKGVR
     VAVIDTGVDV RHPQLKAAVD TKSGVNLIPK DAKDEHGNKV DRGKEDGTTD TVGHGTKVAG
     IIAARPAPGT GFVGLAPDAT IIPIQQNDAT GNGTAKTLAT AIQHAIDEKA DVINISQDTA
     NAIEPTPLLK QAVQKALDAE IVVVASAGND GIDGTDKKTY PASYEGVLAV AASDRNNERA
     AFSQSGDFVG IAAPGVDMIT TVPGGGHCAD NGTSFSAPYV AAVAALVKAK HGDWTQEQIV
     AQLQQTAERS VAGHDRLVGW GVVDPVRALT EDDKPLEAPV AHEGVTKAEP PTPAALHLGE
     TPEQRDARLA TYVVVGGGVL VAAIAGIAVA IRDARRRGSA RTANG
//