ID A0A0R2DRT0_9LACO Unreviewed; 446 AA.
AC A0A0R2DRT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Trypsin-like serine protease {ECO:0000313|EMBL:KRN02660.1};
GN ORFNames=FD13_GL001651 {ECO:0000313|EMBL:KRN02660.1};
OS Levilactobacillus senmaizukei DSM 21775 = NBRC 103853.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423803 {ECO:0000313|EMBL:KRN02660.1, ECO:0000313|Proteomes:UP000051589};
RN [1] {ECO:0000313|EMBL:KRN02660.1, ECO:0000313|Proteomes:UP000051589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21775 {ECO:0000313|EMBL:KRN02660.1,
RC ECO:0000313|Proteomes:UP000051589};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN02660.1}.
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DR EMBL; AYZH01000005; KRN02660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2DRT0; -.
DR STRING; 1423803.FD13_GL001651; -.
DR PATRIC; fig|1423803.3.peg.1703; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000051589; 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:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
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; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KRN02660.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 332..420
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 45936 MW; 4F81FBFDC5D6BE96 CRC64;
MMDNNNNNDQ INDNNNEETP TSAPQGRKRG KLTLTKVAIT AVVAGLLGGG VAYGGISYIN
NSGINDTAVP SGSNKSGNAS TSNVTVNVNT QSTKAFNQVK GAMVSVINLQ KENSNNSTLG
QLFGENSSSS SSSSKSQLEE ASEGSGVVYK KSGSTAYIVT NNHVVSGSSA LRVVTSSGKQ
LQAKVVGKDS VTDLAVLKVN GSDLKTVASF GNSDKVKVGE TALAIGSPLG SQYATSLTQG
IISAKKRTIE TTNSAGTQTG NATVIQTDAA INPGNSGGAL INVGGQVVGI TSSKIASDTE
GTSVEGMGFA IPSNEVVNII NQLVKKGKVV RPALGITYVD LANVSSSQQK SVLKLPSNVD
SGVVVMSAST GSPAKNAGLA KYDVITELGG QKITNQSTLR DLLYKYKIND TVSMTYYHNG
KKQTTKVKLT ETSSQLKTST NANSES
//
