ID A0A285QKB0_9ACTN Unreviewed; 544 AA.
AC A0A285QKB0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Type VII secretion-associated serine protease mycosin {ECO:0000313|EMBL:SOB82395.1};
GN ORFNames=SAMN06272789_2558 {ECO:0000313|EMBL:SOB82395.1};
OS Streptomyces sp. 1331.2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB82395.1, ECO:0000313|Proteomes:UP000219030};
RN [1] {ECO:0000313|Proteomes:UP000219030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA Varghese N., Submissions S.;
RL Submitted (JUL-2017) 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; OBMJ01000001; SOB82395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285QKB0; -.
DR Proteomes; UP000219030; 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; 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.
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:UP000219030};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 484..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 143..405
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 389..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 186
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 356
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 544 AA; 56263 MW; 54D2B941B1A97492 CRC64;
MSRWVRRPWS PRQGRVVRRR SWRASLPGWC WWPAWCSCWC GGGSRPCSLR PLFRWCRRIS
RCRRRTSRRC RRRTIRTRGS RGASVVGDRV GNRWTRRFVA VGVASLWVAG ALAGPAAADE
TVRARQWHLD AMHAPEMWKT STGQGVTVAV IDGGFRLDHP DLVGQFLPGK DFSGSPGGVG
TFGDGHGTEM SSLIAGTGKG VGGTGAYGLA PGAKILPLKI NNGSVGALVS ADFLDQIGQA
VNYAVDQGAK VINISQGIAA VTAMPSDVDK LDRILAAARS KGVLVVSSVG NKAQSGNLLS
YPGGLPNVVG VGAIDRQGTV TAESETGPHV ALVAPGDEIL AGCTSETEYC KSHGTSDAAA
LVSASAALVW AVHKDWTANQ VLRVLINTAG RPNGGDKRTD DAGWGAVRPR VALTDPGDPG
PAGVSPLPAD AVLPSAAPSG SASASASAPV SSVPSAAGSP TDVAVGAPPV QPKADSSSGS
GSSLPIVAGV VAGLVLVAGV VFVVVRRRKS AVQPEVAVPP VPPQQPLPPS YQPPVPPEDN
PYAR
//