ID A0A0M2SRS6_9BACI Unreviewed; 411 AA.
AC A0A0M2SRS6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KKK36843.1};
GN ORFNames=WQ57_16945 {ECO:0000313|EMBL:KKK36843.1};
OS Mesobacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK36843.1, ECO:0000313|Proteomes:UP000034166};
RN [1] {ECO:0000313|EMBL:KKK36843.1, ECO:0000313|Proteomes:UP000034166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA2-6 {ECO:0000313|EMBL:KKK36843.1,
RC ECO:0000313|Proteomes:UP000034166};
RA Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) 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:KKK36843.1}.
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DR EMBL; LAYY01000021; KKK36843.1; -; Genomic_DNA.
DR RefSeq; WP_046524955.1; NZ_LAYY01000021.1.
DR AlphaFoldDB; A0A0M2SRS6; -.
DR PATRIC; fig|1408103.3.peg.3774; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000034166; 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.
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:KKK36843.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034166};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 304..393
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 411 AA; 44089 MW; 418AE16E508E44D2 CRC64;
MGYYDNDHTR NQRKKGSRGG YFLTSLAGAL IGGLLIIFST PLLSEYGLLP YKVEPQNGSA
QPDSRDESPG ESKNISVDVV TEVTKAVEKT GSAVVGITNI QTGGGFWFGS AQGQEAGTGS
GVIYKKEGDN AYVVTNYHVI EGANELEVSL SDGTKVPATL KGGDEWTDLA VLEISAENVE
TVAEFGDSDN LKIGEPAIAI GNPLGLRFSN SVTQGIISGL ERAIPVDINQ DGQPDWQAEV
LQTDAAINPG NSGGALINID GQVIGINSMK IAQSAVEGIG LAIPINYAIP IIEDLEEHGT
VKRPYMGIQL GSVNQIPERY QQSELNLPKD VNYGVAVLDV TENSPAQEAG LQAYDVIVEL
DGEKIEDVVA LRKHLYNEKE PGEEMQISFY RDGKLQETTM TLVEDKMTIE Q
//