ID   A0A1G8JYD3_9BACL        Unreviewed;       485 AA.
AC   A0A1G8JYD3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Trypsin-like peptidase domain-containing protein {ECO:0000313|EMBL:SDI36201.1};
GN   ORFNames=SAMN04487975_11571 {ECO:0000313|EMBL:SDI36201.1};
OS   Planococcus glaciei.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=459472 {ECO:0000313|EMBL:SDI36201.1, ECO:0000313|Proteomes:UP000183022};
RN   [1] {ECO:0000313|Proteomes:UP000183022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6846 {ECO:0000313|Proteomes:UP000183022};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNDC01000015; SDI36201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8JYD3; -.
DR   STRING; 459472.SAMN04487975_11571; -.
DR   eggNOG; COG0265; Bacteria.
DR   OrthoDB; 189537at2; -.
DR   Proteomes; UP000183022; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          58..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  53907 MW;  83B9440B79FADB1B CRC64;
     MLCNKCGQEN DVNANFCKSC GHSLSNNASK KEKRKKWMYS LILLIGLGGA GFGASQLMQE
     PPQQAAPSEE LSSAKEDEQE EKQEQQEQEQ EQAEKQGQEQ SEEPEEIKEP VELAASEGKT
     EGTVTKVEDI VPPSEQPEKV EPKKKDKPAI IKDTQQKVYT ILTEGGQGSG FLFHQSGLVA
     TNAHVVAGFT DVIVRNINGQ DQPGTVVGIS DESDIALIKV DAFAGIDPLE SEMNPTDVGT
     EVIALGSPSG FENTATIGYL TGIDRDFEQE FIYEDIYQID APIAPGSSGG PLVDASTGKV
     IGINSLVMEE GNSIGFSIPL YSMHGMLTEW VNNPMSAEEV VAKFHVYDDF SGYEDENYEF
     DPDLEMKFEE SSLHEFVGDF RYYYETALAE EDFFYVQNLL VYESDIYNGI LEYIGDIAGK
     EMEFNFNKLE ITGTEIFEDH ALVHTEEAFD FKNEAGEWSL EERSKTYTIV MDENGFYYVS
     DIVNK
//