ID A0A327YJZ9_9BACI Unreviewed; 428 AA.
AC A0A327YJZ9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Serine protease Do {ECO:0000313|EMBL:RAK20546.1};
GN ORFNames=B0I26_104199 {ECO:0000313|EMBL:RAK20546.1};
OS Anoxybacillus vitaminiphilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=581036 {ECO:0000313|EMBL:RAK20546.1, ECO:0000313|Proteomes:UP000248555};
RN [1] {ECO:0000313|EMBL:RAK20546.1, ECO:0000313|Proteomes:UP000248555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8979 {ECO:0000313|EMBL:RAK20546.1,
RC ECO:0000313|Proteomes:UP000248555};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) 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:RAK20546.1}.
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DR EMBL; QLMH01000004; RAK20546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327YJZ9; -.
DR Proteomes; UP000248555; 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; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RAK20546.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 313..389
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 428 AA; 46307 MW; 569A73595E0F7C05 CRC64;
MVVRYIHYLL LKASSSMKGL VSTVGYYDDH YQQYQQKQKG NRGGTFLAAL VGAILGALLI
MFSIPTLSKW NVLPYDIAIK GDENEMKEDM SQKPVVQKSV AVDVVSQVTK AVDKVSDAVV
GVVNIQEASF WSQGGEAGTG SGVIYKKANG KAFIVTNHHV VENASQIEVS LKDGTRVPAK
LLGSDVLTDL AVLEIDAKHV KKVAEFGNSD VVKPGEPVIA IGSPLGLQFA GSVTQGIISG
TNRTIEVDLD QDGMPDWNAE VLQTDAAINP GNSGGALVNI EGQVIGINSM KIAQEAVEGI
GFSIPINFAQ PIIADLEKYG QVRRPYMGVE LRSLSDISSY HLQETLHLPE DVTEGVAIVQ
VVPMSPAAQA GLKQFDVIVA LDDKPIRNVL ELRKYLYTEK SIGDEMKVTF YREGKKQTVT
MKLAKESF
//
