ID A0A1H1FX38_9BACI Unreviewed; 430 AA.
AC A0A1H1FX38;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=HtrA-like peptidase. Serine peptidase. MEROPS family S01B {ECO:0000313|EMBL:SDR05329.1};
GN ORFNames=SAMN05216231_3457 {ECO:0000313|EMBL:SDR05329.1};
OS Virgibacillus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=553311 {ECO:0000313|EMBL:SDR05329.1, ECO:0000313|Proteomes:UP000199444};
RN [1] {ECO:0000313|EMBL:SDR05329.1, ECO:0000313|Proteomes:UP000199444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10449 {ECO:0000313|EMBL:SDR05329.1,
RC ECO:0000313|Proteomes:UP000199444};
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; FNKD01000004; SDR05329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1FX38; -.
DR STRING; 553311.SAMN05216231_3457; -.
DR Proteomes; UP000199444; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199444};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 316..416
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 45991 MW; B5E6296C67FD4016 CRC64;
MDRNDNDNNK ELEENTLDKQ EQKTEANPGI AETARQNAKP KQDKPKQKSG VKTLMSGIAG
GVISAVIVAL LFTTNIIPLN QQENSNSASS ESNEQTAPEI AETVSSDSSN IASNMDEASK
AVVGVINKQQ QSVWTQSQQA GAGSGIIYKE KDGKAYVVTN QHVVKGAEEV EIVLNKDTRI
SAKVLGTDSF TDLAVLQIDG KKVNTVADLG SSKNLKVGDT VVAIGNPLGM NFANSVTKGI
ISGLDRSVSI DTNGDGQPDW ITEVIQTDAA INPGNSGGAL INSKGEVIGI NSMKIAKTSV
EGIGFSIPID EAQPIMKQLE KDGEVARPFI GISTASMGQV PPQYRDQIQL PENVEGGMVV
AKVQQGSPAS QAELQQFDVI TKINGNKITS ILDLRKYLYN ETKIGESVEL EIYRDGEPQK
IALELVKREQ
//
