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Database: UniProt
Entry: A0A1I0XUR0_9BACI
LinkDB: A0A1I0XUR0_9BACI
Original site: A0A1I0XUR0_9BACI 
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
//
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