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Database: UniProt
Entry: A0A248TEE7_9BACI
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ID   A0A248TEE7_9BACI        Unreviewed;       412 AA.
AC   A0A248TEE7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Peptidase S1 {ECO:0000313|EMBL:ASV66575.1};
GN   ORFNames=CKF48_04100 {ECO:0000313|EMBL:ASV66575.1};
OS   Cytobacillus kochii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX   NCBI_TaxID=859143 {ECO:0000313|EMBL:ASV66575.1, ECO:0000313|Proteomes:UP000215137};
RN   [1] {ECO:0000313|EMBL:ASV66575.1, ECO:0000313|Proteomes:UP000215137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDGP4 {ECO:0000313|EMBL:ASV66575.1,
RC   ECO:0000313|Proteomes:UP000215137};
RA   Wan K.H., Yu C., Park S., Hammonds A.S., Booth B.W., Celniker S.E.;
RT   "Complete Genome Sequence of Bacillus kochii Oregon-R-modENCODE STRAIN
RT   BDGP4, isolated from Drosophila melanogaster gut.";
RL   Submitted (AUG-2017) 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; CP022983; ASV66575.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248TEE7; -.
DR   KEGG; bko:CKF48_04100; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000215137; Chromosome.
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.
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:UP000215137};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          306..392
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   REGION          104..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  44174 MW;  E329717CDD33B5AD CRC64;
     MNEFNHFEDN REYQSKRKNT WFKSVTMTVA SGVMGSALTL GAINYFPNET KQSTEVVQEQ
     AETNVSKVNA ETVSTTSDGS IADIVEKASK AIVGVVNMQE QQANPFSHST GNTQSGEAVE
     SGTGSGVIFK QTDNETYIVT NNHVIEGASN IQVSLHNGEK LQAELVGTDS LTDIAVLKVN
     EKVDAEVLSF TDSSNLRAGD QVLAIGNPLG LDLSRTVTQG IVSAVDRSIE VSTSAGEWDL
     NVIQTDAAIN PGNSGGALID SNGNLVGINS LKIADSGVEG LGFAIPSNDV ENIIDQLMKD
     GKIIRPYLGV GLMDLNQVPQ FYQEQLPKNV EEGAIITQVE EGSTAETAGL QAEDILVSIG
     DQTITAANDL RESLYKDFSI GDKVKIYFYR DGEKKTVEVT LQGNGEKQVE KE
//
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