ID A0A1H0WL68_9PSEU Unreviewed; 398 AA.
AC A0A1H0WL68;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Type VII secretion-associated serine protease mycosin {ECO:0000313|EMBL:SDP91305.1};
GN ORFNames=SAMN05421507_12047 {ECO:0000313|EMBL:SDP91305.1};
OS Lentzea jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=641025 {ECO:0000313|EMBL:SDP91305.1, ECO:0000313|Proteomes:UP000199691};
RN [1] {ECO:0000313|EMBL:SDP91305.1, ECO:0000313|Proteomes:UP000199691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6609 {ECO:0000313|EMBL:SDP91305.1,
RC ECO:0000313|Proteomes:UP000199691};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; FNIX01000020; SDP91305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0WL68; -.
DR STRING; 641025.SAMN05421507_12047; -.
DR OrthoDB; 5240330at2; -.
DR Proteomes; UP000199691; 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; 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.
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};
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 348..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..298
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 312..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..331
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 59
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 94
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 250
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 398 AA; 40314 MW; DBE79D855CF6303C CRC64;
MTWKDDVAGV ALLPALTVAL PLLLAAQTIE EQEWHLDALD VYSAQAQARG DGVVVAVIDS
GVDAQHPDLV GQVLPGTGFG SSKGTDGTTD TDGHGTAMAG IIAAAGRDGG ALGIAPGVKI
LPVASAEREQ FTLDVVAESI RWAADHGAKV INMSLGFSSS MTPTLVKAVN YAIEKDVVLV
AATGNEGRAV SAPANIQGVI AVSGTTRDGK PWASSNVGAD TVLSAPAAGI VTASPKSVYP
SGYAEVDGTS AASAIVAGVA ALVRAKHPRM PAKDVVNALI KSAKDLAEPG RDATTGFGVV
DPVGALNAQL PPVERHPLLP PPKPPTTKPA PTPARTAQRP DVDLGSRMPF IAAVAGGTAV
MTGLLITLPA IRSRRPRPQA TVHVLPPLSG SGTPPTPW
//
