ID   HTRA_LACLA              Reviewed;         408 AA.
AC   Q9LA06;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Serine protease Do-like HtrA;
DE            EC=3.4.21.107;
GN   Name=htrA; OrderedLocusNames=LL2136; ORFNames=L187771;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A HOUSEKEEPING PROTEASE, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=IL1403;
RX   PubMed=10712686; DOI=10.1046/j.1365-2958.2000.01757.x;
RA   Poquet I., Saint V., Seznec E., Simoes N., Bolotin A., Gruss A.;
RT   "HtrA is the unique surface housekeeping protease in Lactococcus lactis and
RT   is required for natural protein processing.";
RL   Mol. Microbiol. 35:1042-1051(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
RN   [3]
RP   FUNCTION IN THE RESPONSE TO SPECIFIC STRESS CONDITIONS, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12855167; DOI=10.1016/s0378-1097(03)00419-1;
RA   Foucaud-Scheunemann C., Poquet I.;
RT   "HtrA is a key factor in the response to specific stress conditions in
RT   Lactococcus lactis.";
RL   FEMS Microbiol. Lett. 224:53-59(2003).
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. {ECO:0000269|PubMed:10712686,
CC       ECO:0000269|PubMed:12855167}.
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   -!- INDUCTION: Induced during stress conditions.
CC       {ECO:0000269|PubMed:12855167}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation leads to growth thermo-sensitivity
CC       and reduce the efficiency of secretion of the recombinant protein
CC       produced, although the protein produced is completely stabilized. Cells
CC       lacking this gene show an alteration of surface properties.
CC       {ECO:0000269|PubMed:10712686, ECO:0000269|PubMed:12855167}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR   EMBL; AF155705; AAF61294.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK06234.1; -; Genomic_DNA.
DR   PIR; H86891; H86891.
DR   RefSeq; NP_268293.1; NC_002662.1.
DR   RefSeq; WP_010906329.1; NC_002662.1.
DR   AlphaFoldDB; Q9LA06; -.
DR   SMR; Q9LA06; -.
DR   STRING; 272623.L187771; -.
DR   MEROPS; S01.447; -.
DR   PaxDb; Q9LA06; -.
DR   EnsemblBacteria; AAK06234; AAK06234; L187771.
DR   KEGG; lla:L187771; -.
DR   PATRIC; fig|272623.7.peg.2295; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_0_2_9; -.
DR   OMA; SSYPEQD; -.
DR   BRENDA; 3.4.21.107; 2903.
DR   Proteomes; UP000002196; 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   GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Serine protease; Stress response; Transmembrane; Transmembrane helix.
FT   CHAIN           1..408
FT                   /note="Serine protease Do-like HtrA"
FT                   /id="PRO_0000093861"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          302..383
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        127
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        157
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        239
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   BINDING         237..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         298..302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  41648 MW;  581B90B55A7DF851 CRC64;
     MAKANIGKLL LTGVVGGAIA LGGSAIYQST TNQSANNSRS NTTSTKVSNV SVNVNTDVTS
     AIKKVSNSVV SVMNYQKDNS QSSDFSSIFG GNSGSSSSTD GLQLSSEGSG VIYKKSGGDA
     YVVTNYHVIA GNSSLDVLLS GGQKVKASVV GYDEYTDLAV LKISSEHVKD VATFADSSKL
     TIGEPAIAVG SPLGSQFANT ATEGILSATS RQVTLTQENG QTTNINAIQT DAAINPGNSG
     GALINIEGQV IGITQSKITT TEDGSTSVEG LGFAIPSNDV VNIINKLEAD GKISRPALGI
     RMVDLSQLST NDSSQLKLPS SVTGGVVVYS VQSGLPAASA GLKAGDVITK VGDTAVTSST
     DLQSALYSHN INDTVKVTYY RDGKSNTADV KLSKSTSDLE TSSPSSSN