ID   A8YWL1_LACH4            Unreviewed;       413 AA.
AC   A8YWL1;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=HtrA-like serine protease {ECO:0000313|EMBL:ABX26373.1};
GN   OrderedLocusNames=lhv_0100 {ECO:0000313|EMBL:ABX26373.1};
OS   Lactobacillus helveticus (strain DPC 4571).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=405566 {ECO:0000313|EMBL:ABX26373.1, ECO:0000313|Proteomes:UP000000790};
RN   [1] {ECO:0000313|EMBL:ABX26373.1, ECO:0000313|Proteomes:UP000000790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 4571 {ECO:0000313|EMBL:ABX26373.1,
RC   ECO:0000313|Proteomes:UP000000790};
RX   PubMed=17993529; DOI=10.1128/JB.01295-07;
RA   Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA   McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA   Beresford T., Ross R.P.;
RT   "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT   selective gene loss and IS element expansion.";
RL   J. Bacteriol. 190:727-735(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; CP000517; ABX26373.1; -; Genomic_DNA.
DR   RefSeq; WP_012211251.1; NC_010080.1.
DR   AlphaFoldDB; A8YWL1; -.
DR   MEROPS; S01.447; -.
DR   KEGG; lhe:lhv_0100; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_0_2_9; -.
DR   Proteomes; UP000000790; Chromosome.
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; 2.40.10.10; 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.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABX26373.1};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          305..401
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   413 AA;  42633 MW;  B16EC77A31CE8707 CRC64;
     MVENQNNNQN QPRKKSGNKI IATAAIFGVV GGLVGGGVSY YAMDQMNNGQ GNGAAQISIS
     SSSSKVSEKS AKNGGTMTAA YNDVKGAVVS VINLKRQSAS SGTDSLYNSL FGDDSDSSSS
     KNGKLETYSE GSGVVYMKSN GKGYIVTNNH VISGSDAVQV LLANGKTVNA KVVGKDSTTD
     LAVLSIDAKY VTQTAQFGDS KHLEAGQTVI AVGSPLGSEY ASTVTQGIIS APARTISTSS
     GNQQTVIQTD AAINPGNSGG ALVNSAGQVI GINSMKLAQS SDGTSVEGMG FAIPSNEVVT
     IVNELVKKGK ITRPQLGVRV IALQGIPEGY RSRLKIKSNL KNGIYIAFVS RNGSAANAGI
     KSGDVITKVD GKKVEDVASL HSILYSHKVG DTVNVTVNRN GKDVDMKVKL EGN
//