ID A0A1Q9Q019_9BACI Unreviewed; 388 AA.
AC A0A1Q9Q019;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Peptidase S1 {ECO:0000313|EMBL:OLS39979.1};
GN ORFNames=BTR25_12010 {ECO:0000313|EMBL:OLS39979.1};
OS Bacillus sp. MRMR6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1928617 {ECO:0000313|EMBL:OLS39979.1, ECO:0000313|Proteomes:UP000185615};
RN [1] {ECO:0000313|EMBL:OLS39979.1, ECO:0000313|Proteomes:UP000185615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRMR6 {ECO:0000313|EMBL:OLS39979.1,
RC ECO:0000313|Proteomes:UP000185615};
RA Thomas J.M., Ghebrendrias N., Rawat M.;
RT "Mendota Genome Annoucement.";
RL Submitted (DEC-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}.
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:OLS39979.1}.
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DR EMBL; MSLS01000010; OLS39979.1; -; Genomic_DNA.
DR RefSeq; WP_075688363.1; NZ_MSLS01000010.1.
DR AlphaFoldDB; A0A1Q9Q019; -.
DR STRING; 1928617.BTR25_12010; -.
DR Proteomes; UP000185615; 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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000185615};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 285..353
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 388 AA; 41115 MW; C55BD3F1E5C09631 CRC64;
MKKSNKKKNL KGFASTLAAG IIGSVLTLTI LPHTDYIKNF TNVESQSIGS KQLEGTSTVK
AVPTSAVTNT SSIADTVEQL SKTIVGVVNY QQLQNRSIYG NSSSQSIQSG TGSGVIFQKN
KDTAYIVTNN HVVEGASKLE ISLYNGEKVE GEIVGTDALT DLAVLKIDAK YVDATAEFGD
SSSLRPGDQV FAIGNPLGLD LSRTVTQGIV SAINRSISIE TSAGNWETNV IQTDAAINPG
NSGGALINPQ GLVIGINSLK ISNSGVEGLG FAIPSNDLIP IVNELINNGK IERPYLGVGL
ADLEQIPQLY WPNNVSEGVI ITTVEPNSAA ANAGLQVKDV IVSMNDTKIK TASELRRFLY
TKVKVGDEVK VEVYRDGEST TLTVNLNK
//