ID A0A1I0XUR0_9BACI Unreviewed; 443 AA.
AC A0A1I0XUR0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Serine protease Do {ECO:0000313|EMBL:SFB04741.1};
GN ORFNames=SAMN04488072_10635 {ECO:0000313|EMBL:SFB04741.1};
OS Lentibacillus halodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=237679 {ECO:0000313|EMBL:SFB04741.1, ECO:0000313|Proteomes:UP000198642};
RN [1] {ECO:0000313|EMBL:SFB04741.1, ECO:0000313|Proteomes:UP000198642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3702 {ECO:0000313|EMBL:SFB04741.1,
RC ECO:0000313|Proteomes:UP000198642};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; FOJW01000006; SFB04741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0XUR0; -.
DR STRING; 237679.SAMN04488072_10635; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000198642; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0000256|ARBA:ARBA00022825};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFB04741.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198642};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..425
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 47073 MW; 27BEA719F8CC2DEA CRC64;
MDNNHYQHDN EHTDDTHQAY PESEPVKKAD SNPNGGIAQT ARQNAQANQT EKPKRNRSGH
LFSGLIGGLV SAIVVVLLFN TNIISDNDGN NSSDAASTEN GQGSGAPEVT ETMASDDANV
ASNLDEASKA VVGVTRMEQT NVWEPSQESG TGSGIIYKKE DGNAYVVTNQ HVVADAQEVE
VALNNDERIE AEVLGSDELS DLAVLKIDGS QIDTVANLGS SSDVEVGETA VAIGNPLGME
FANTLTRGII SGLDRSVNMD TNGDSQPDWV TEVIQTDAAI NPGNSGGALV NADGKVIGIN
SMKIAQTAVE GIGFAIPIDT AMPIIEQLET DGKISRPYIG ISTASINQVP PQYRNQIQLP
EDVEEGIVIA QVETGSPADD ANLQQFDVVT KINGNNVTSL VDLRQYLYNE AEIGGTIELE
VYRNGEAQTV TLDLAERGQE QQQ
//