ID   HTRA_LACLM              Reviewed;         407 AA.
AC   A2RNT9;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Serine protease Do-like HtrA;
DE            EC=3.4.21.107;
GN   Name=htrA; OrderedLocusNames=llmg_2419;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18836019; DOI=10.1128/aem.00638-08;
RA   Sriraman K., Jayaraman G.;
RT   "HtrA is essential for efficient secretion of recombinant proteins by
RT   Lactococcus lactis.";
RL   Appl. Environ. Microbiol. 74:7442-7446(2008).
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   -!- DISRUPTION PHENOTYPE: Inactivation leads to reduce the efficiency of
CC       secretion of the recombinant protein produced, although the protein
CC       produced is completely stabilized. {ECO:0000269|PubMed:18836019}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR   EMBL; AM406671; CAL98983.1; -; Genomic_DNA.
DR   RefSeq; WP_011836058.1; NZ_WJVF01000024.1.
DR   AlphaFoldDB; A2RNT9; -.
DR   SMR; A2RNT9; -.
DR   STRING; 416870.llmg_2419; -.
DR   MEROPS; S01.447; -.
DR   EnsemblBacteria; CAL98983; CAL98983; llmg_2419.
DR   KEGG; llm:llmg_2419; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_0_2_9; -.
DR   OMA; DTRHFDY; -.
DR   PhylomeDB; A2RNT9; -.
DR   BioCyc; LLAC416870:LLMG_RS12130-MON; -.
DR   Proteomes; UP000000364; Chromosome.
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..407
FT                   /note="Serine protease Do-like HtrA"
FT                   /id="PRO_0000414027"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          301..382
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        126
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        156
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         236..238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         297..301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  41541 MW;  9FEE80E8BC030BF3 CRC64;
     MAKANIGKLL LTGVVGGAIA LGGSAIYQST TNQLGNANRS NTTSTKVSNV SVNVNTDVTS
     AIKKVSNSVV SVMNYQKQNS QSDFSSIFGG NSGSSSANDG LQLSSEGSGV IYKKSGGDAY
     VVTNYHVIAG NSSLDVLLSG GQKVKATVVG YDEYTDLAVL KISSDHVKDV ATFADSSKLT
     IGEPAIAVGS PLGSQFANTA TEGILSATSR QVTLTQENGQ TTSINAIQTD AAINPGNSGG
     ALINIEGQVI GITQSKITTT EDGSTSVEGL GFAIPSNDVV NIINKLETDG KISRPALGIR
     MVDLSQLSTN DSSQLKLPSS VTGGVVVYSV QAGLPAATAG LKAGDVITKV GDTAVTSSTD
     LQSALYSHNI NDTVKVTYYR DGKSATANVK LSKSTSDLET NSSSSSN