HTRA_LACHE
ID HTRA_LACHE Reviewed; 413 AA.
AC Q9Z4H7;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine protease Do-like HtrA;
DE EC=3.4.21.107;
GN Name=htrA;
OS Lactobacillus helveticus (Lactobacillus suntoryeus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=53/7;
RX PubMed=9829922; DOI=10.1128/jb.180.23.6148-6153.1998;
RA Smeds A., Varmanen P.K., Palva A.M.;
RT "Molecular characterization of a stress-inducible gene from Lactobacillus
RT helveticus.";
RL J. Bacteriol. 180:6148-6153(1998).
CC -!- FUNCTION: Degrades abnormal exported proteins and responsible for the
CC propeptide processing of a natural pro-protein and for the maturation
CC of a native protein. It also plays a prominent role in stress (heat
CC shock, ethanol, puromycin and NaCl) resistance during active
CC exponential growth (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AJ005672; CAA06668.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Z4H7; -.
DR SMR; Q9Z4H7; -.
DR STRING; 326425.lhe_0111; -.
DR MEROPS; S01.447; -.
DR eggNOG; COG0265; Bacteria.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; -; 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 Pfam; PF13180; PDZ_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Protease; Serine protease;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..413
FT /note="Serine protease Do-like HtrA"
FT /id="PRO_0000093860"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 305..401
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT BINDING 256..258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 316..320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 413 AA; 42647 MW; B16B677991C88707 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 SDGTSVEGMA FAIPSNEVVT
IVNELVKKGK ITRPQLGVRV IALQGIPEGY RSRLKIKSNL KNGIYIAFVS RNGSAANAGI
KSGDVITKVD GKKVEDVASL HSILYSHKVG DTVNVTVNRN GKDVDMKVKL EGN