ID A0A0X3UT66_9ACTN Unreviewed; 540 AA.
AC A0A0X3UT66;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KUL35779.1};
GN ORFNames=ADL15_13505 {ECO:0000313|EMBL:KUL35779.1};
OS Actinoplanes awajinensis subsp. mycoplanecinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL35779.1, ECO:0000313|Proteomes:UP000053244};
RN [1] {ECO:0000313|EMBL:KUL35779.1, ECO:0000313|Proteomes:UP000053244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL35779.1,
RC ECO:0000313|Proteomes:UP000053244};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUL35779.1}.
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DR EMBL; LLZH01000097; KUL35779.1; -; Genomic_DNA.
DR RefSeq; WP_067689268.1; NZ_LLZH01000097.1.
DR AlphaFoldDB; A0A0X3UT66; -.
DR OrthoDB; 8781117at2; -.
DR Proteomes; UP000053244; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd21112; alphaLP-like; 1.
DR Gene3D; 3.30.300.50; -; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR004236; Pept_S1_alpha_lytic.
DR InterPro; IPR001316; Pept_S1A_streptogrisin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR035070; Streptogrisin_prodomain.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF02983; Pro_Al_protease; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00861; ALYTICPTASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KUL35779.1};
KW Protease {ECO:0000313|EMBL:KUL35779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053244};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007055274"
FT DOMAIN 127..182
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 204..380
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT REGION 343..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 54403 MW; 441A78D21B8970B2 CRC64;
MQRRSIAVAA AVVAATAAAV AFTLPSMADT TPAGDSSGTT KASGGVSPDL LAAMKRDLGL
DAAQATTRLN RSKWAGGVSA TLAAATGDDY AGAWLAADGT TLKVAVTDPD AVAVVKKAGA
VPVLVKRSEA QLDAAKTKLD DALAKAGDLT GWYVDAPTNK LVVVAQPGDK AAAQTFARRA
GLSSDAITVK ISNQQPKPLF DVRGADPYFI AVDGGTARCS IGFSVEGGFV TAGHCGTPGT
TTTGFNNEAQ GVVKASVFPG DADMGFVEVN GDWTPRPVVN DFKGNELPVA GNTEAPIGAA
VCRSGSTTGT FCGTILAKNQ TVVYPEGAVT GLTRTDVCAE GGDSGGPWLS GDQAQGVTSG
GSGDCTVGGE TFFQPVNEIL AADELTLVTT GAEEGGATAA PTDAATVAPS EEAPPSEEAP
PSEEAPPSEE APPAEEASEC AALPVQRTGS LTKSGTAQAQ PNNGAFRARA GEHVACLDSP
DGADFDLVLQ RKTDHGFKTV ATAKGDDVKT LSVNQRSGTF RYVVVASSGS GDYALGFNVQ
//