ID   A0A1I1BMN7_9PSEU        Unreviewed;       501 AA.
AC   A0A1I1BMN7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Serine protease, S1-C subfamily, contains C-terminal PDZ domain {ECO:0000313|EMBL:SFB51659.1};
GN   ORFNames=SAMN05216266_115132 {ECO:0000313|EMBL:SFB51659.1};
OS   Amycolatopsis marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=490629 {ECO:0000313|EMBL:SFB51659.1, ECO:0000313|Proteomes:UP000243799};
RN   [1] {ECO:0000313|Proteomes:UP000243799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3568 {ECO:0000313|Proteomes:UP000243799};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; FOKG01000015; SFB51659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1BMN7; -.
DR   STRING; 490629.SAMN05216266_115132; -.
DR   Proteomes; UP000243799; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:SFB51659.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SFB51659.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243799};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        153..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          403..489
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  50527 MW;  A11A89571D2C3AC4 CRC64;
     MRENRLGPRP VQRPAVDPAQ AATFGRPQGV TGAFDKLYAP DSGPRRDGST GNGVTLAPPP
     PESLAEAFRR PPGADGVVLQ RPNDGNGTTA EDPEDPLWAE PADPWRDPGA GAVLGRPAVQ
     AEEASAGAEK RPSGALLSLP EVLFGRRVKP RALALLGVVA LLVGAAGGLV GWGLASAGNS
     LTGELNIAEA QAGKERPAGS IAEITRRVAP AVVSIEVKAG QSGGVGSGVV IDPEGYVLTN
     NHVVALAAED EEAEITAVFT DGTRGSAQIV GLDPKTDLAV IKVAVSNPIV IEIGSSSELA
     AGDTVIAVGS PFGLENTVTE GIVSALNRPV TAPGENGDPP VTYDAIQTDA AINPGNSGGA
     LVDATGALVG INSLIRTVGG AEGEGGSIGL GFAIPVDQAI KIAESLIRDG QVKHPDIGVN
     AASVAANTSE GAQIQNVAEG GPADRAGIAE GDVVTKVGDR TVRNAAELTV AIRQHEIGDV
     VPVRIVRQGR PLTVDVTLGS D
//