ID A0A1C6QM12_9ACTN Unreviewed; 430 AA.
AC A0A1C6QM12;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Type VII secretion-associated serine protease mycosin {ECO:0000313|EMBL:SCK56666.1};
GN ORFNames=H181DRAFT_05285 {ECO:0000313|EMBL:SCK56666.1};
OS Streptomyces sp. WMMB 714.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1286822 {ECO:0000313|EMBL:SCK56666.1, ECO:0000313|Proteomes:UP000182206};
RN [1] {ECO:0000313|Proteomes:UP000182206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMB 714 {ECO:0000313|Proteomes:UP000182206};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; FMHJ01000018; SCK56666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6QM12; -.
DR STRING; 1286822.GCA_000964305_05251; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000182206; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000182206};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..430
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008744120"
FT TRANSMEM 352..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..300
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 381..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 62
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 430 AA; 44942 MW; B4942E0416852EFD CRC64;
MGKRPTLRVI GSTAIAGVLI FAASPQAVAD DVRDKQWALD ALDAESVWKV TRGKGQTIAV
IDDGVNAQHP DLKGNVLKGK DFVDGGSPAP ERGDSHGTGM AAMIAGHGHG PGNANGIMGL
APAAKILPIR VTGGKLDDSI KYAVDHGASV INISLGDDSE NSDDDDEAIT YALKKDVPVF
ASTGNSGGAV EYPAAYPGVV PVGGVKQDGT LWEKSNKGPE TLLVGPATRV LTAGGEDSNY
YAYGTGTSDA TAYASATAAL IRAKYPDLAA GQVVNRLAKT AKMPASEKGA KVPDERYGYG
AISPLAALQE DIPKGPKYGP LSLPLEIKNE VEAAKQLKED KALEEKQDRE FVILWTITGV
LAFLFVGAIV LTIVLVRRRR RNRNSGPGGP GAPGGYSYSP NQAPGYGMPS QQQQLYTPES
TAPPQQPPYN
//
