ID   Q2MG30_MICEC            Unreviewed;       430 AA.
AC   Q2MG30;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Putative serine protease, subtilase family {ECO:0000313|EMBL:CAI05919.1};
OS   Micromonospora echinospora (Micromonospora purpurea).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1877 {ECO:0000313|EMBL:CAI05919.1};
RN   [1] {ECO:0000313|EMBL:CAI05919.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 43036 {ECO:0000313|EMBL:CAI05919.1};
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Cloning and sequencing of the gentamicin biosynthetic gene cluster from
RT   Micromonospora echinospora DSM 43036.";
RL   Submitted (FEB-2004) 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; AJ628149; CAI05919.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MG30; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00306; Peptidases_S8_S53; 1.
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   InterPro; IPR006311; TAT_signal.
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; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
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}.
FT   DOMAIN          175..403
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        184
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        226
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        387
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   430 AA;  44826 MW;  45850DEA9EE17E3D CRC64;
     MPCPPGRVSR RRLVGWTMLA AAAVPLGALG RPGLVRAADA LDQAYQRAFL EAVTADPAVR
     RHTTVGREFL YRPRQLLAAP QDLTRVLNRL RSWGHQVTEV TGFGGVRRLL FQQETDIPGV
     VTKLRDPQQW PGQPVPLVQP HHVLLGFGNI MGNPGGPPRV GAALPAPDPA RIGEGAGVTV
     GVCDTGIWRR AGTVHPQWLG GSYLPEADDE DPLYLGGTQL ALQGGHGTFV AGVVRQAAPG
     VRLDPEAALA PTGIGDEESL VAAIRRLRPE VAVVNLSLGY FTQDDQPPLP VANTLAALPA
     TVAVVAAAGN AGTTRKSWPA ALDPVVAVAA VSAGPTGPVP ADYSGRGTWV DASARGDRRS
     TYVDGELYLP GEPAQVFHGF ATWIGTSFAT AHVSGRIAAL MTATGLDAAA AAALLVAGPT
     WQPGYGVLVE
//