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Database: UniProt
Entry: A0A0X9W556_9BACL
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ID   A0A0X9W556_9BACL        Unreviewed;       494 AA.
AC   A0A0X9W556;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Trypsin family protein {ECO:0000313|EMBL:AMA62342.1};
GN   ORFNames=ASO14_2443 {ECO:0000313|EMBL:AMA62342.1};
OS   Kurthia sp. 11kri321.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA62342.1, ECO:0000313|Proteomes:UP000058129};
RN   [1] {ECO:0000313|EMBL:AMA62342.1, ECO:0000313|Proteomes:UP000058129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11kri321 {ECO:0000313|EMBL:AMA62342.1,
RC   ECO:0000313|Proteomes:UP000058129};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP013217; AMA62342.1; -; Genomic_DNA.
DR   RefSeq; WP_068455646.1; NZ_CP013217.1.
DR   AlphaFoldDB; A0A0X9W556; -.
DR   STRING; 1750719.ASO14_2443; -.
DR   KEGG; kur:ASO14_2443; -.
DR   PATRIC; fig|1750719.3.peg.2390; -.
DR   Proteomes; UP000058129; Chromosome.
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   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058129};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   REGION          45..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  54474 MW;  EE6DF3425390FD90 CRC64;
     MSENRRFKPK KAAFKRLVVA FILIAVVAAG IYALVTKTDD QAKDNNIRVQ NEEKEAKKEP
     KDEGEKDAKG TVTKETSNEE TSSKDTTNQD ETPVNMPTYN KDAIIANAKT QIYTVYTDLQ
     QGSGFLINNK GDILTNAHVA KDAGFVVVKN ELGQEFQGKV IGISDKTDVA LIRVPDLEGK
     NPLVLDTATA KVGTKVVAIG SPKDQYGTTT EGVIQSIGAE FVDDYTYKNL YEITARLNKG
     SSGGPLINAE TGNVIGINSI ILEDHPEIGY AIPLASVMGL VNKWSAQDIK IDFNEDTEFD
     NNHADEAYFD ENFLKESMES YYVLLIQSIK NGEHKYYDTF IGNRPAMKEA DAMVSRYTKD
     KQFKSLDYNV TGVTINKDYA TVTMNTVAKY VDPKTKKTHT ITENVAYTII INDIGEYEIS
     SIIVNSSVDT GKQVEEKPVE KPTTPVEKPE VDEPETEEPP TTDGKDDTKT DTEKEDVPAD
     TSSVDSPVDS TTEE
//
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