ID A0A0Q5LNA5_9MICO Unreviewed; 1089 AA.
AC A0A0Q5LNA5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Serine protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASF82_02065 {ECO:0000313|EMBL:KQR46325.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR46325.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR46325.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR46325.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR46325.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR46325.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:KQR46325.1}.
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DR EMBL; LMOX01000001; KQR46325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5LNA5; -.
DR STRING; 1736282.ASF82_02065; -.
DR Proteomes; UP000051005; 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 CDD; cd02120; PA_subtilisin_like; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 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:UP000051005};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1089
FT /note="Serine protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006255780"
FT TRANSMEM 1052..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..141
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 165..659
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 457..522
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 694..788
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 999..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 266
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 606
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1089 AA; 108208 MW; 2C6D24193AA4D04D CRC64;
MYPTALLVTG LVAAGAIALP ATAASAADGP VVVSDSEFTD GSYVVTLRDP AVTAYDGGKS
GFAATATPDE GVDLTDPATS KYVEHLQSEQ EAVAGSVGVT PVATYQVTTN GFAADLTAAQ
AKQLVGSSKV AAVVKNEILH TTAVPSTDYL GLSGADGVWG TQGTGEGVVV GVIDTGIAPE
NPSFAGDALT ATPSDTVPYT TAAGISYEKS DGGTFTGVCQ RGQQFDETDC STKIVGARYF
LAGFGEDRIE TAQNGEYVSP RDGDSHGSHT ASTAAGNADV PVTINGRDFG DISGVAPDAK
VAAYKVCWTG KVSAEVADGC ATADLLSAID AATADNVDVI NYSIGGGSAT STNSLTDQAF
YNAAAAGIFV AASAGNSGPG ASTLDNAAPW ITTVAASTIP SYDATASVTG PDGVVTNYLG
GSTSLSTDPA GVTGRFVDAL SSGLPGVDRT DLSYCTGGTL DPALVTGTIV LCDRGVTDRT
AKSAEVQRAG GIGMVLVNKT PSSVDVDAHV VPTVHVDAGA GNVNYTALHA AAAPGTSTVT
LLDGNPTGQP EPATPQVAGF SSRGPVEADG GNVLKPDVAA PGVAILAAGA NAEGAAATYE
FLSGTSMSSP HVAGLAALYL SVTPTATPME VKSAMMTTAG DTVDTTGAPS QDVFAQGAGQ
VQPADMFDAG LLYLSGVADW DSYIATLGSA EGSQLNQASI AVGALLNSTT VTRTVTSTGA
GTYTAQPVSL PGVATTVSPS TLSFTGAGQT ASYEVTFSRT TAAYDQYTTG YLTWTDGGAH
TVRSPLAVRP VAVDVPSDIT GTGVTGSAEA PITSGGDQTL ALSAEGLVKG ERTSGSGTVG
DFDYVDVTIP ADTQFVRYEL TAGGADAPAV DEPVDFDLTL YELDATGTPV AITATSATSA
ADEQIDITEP EAGSYLLEVA YYSGGETMTY DLDAYTLIPS AYTGSFAVSP TTLTLASNQE
AVVTASWTGL EPESQYLGRI VYGATGRVTY VTVDSGPAVT APVDPGTPAP APGDPGAGAP
GTGAPGAGGA GGTGGGNAAP AASDLAFTGQ DVAPMIAAGV ALLLAGLAAA VIGRRRLRSV
AVTERTPEA
//
