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
//