ID   DEGPL_RICCN             Reviewed;         508 AA.
AC   Q92JA1;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like;
DE            EC=3.4.21.107;
DE   AltName: Full=Protease Do;
DE   Flags: Precursor;
GN   Name=htrA; OrderedLocusNames=RC0166;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- FUNCTION: Might be efficient in the degradation of transiently
CC       denatured and unfolded proteins which accumulate in the periplasm
CC       following stress conditions. {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: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL02704.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE006914; AAL02704.1; ALT_INIT; Genomic_DNA.
DR   PIR; F97720; F97720.
DR   RefSeq; WP_041471707.1; NC_003103.1.
DR   AlphaFoldDB; Q92JA1; -.
DR   SMR; Q92JA1; -.
DR   EnsemblBacteria; AAL02704; AAL02704; RC0166.
DR   KEGG; rco:RC0166; -.
DR   PATRIC; fig|272944.4.peg.195; -.
DR   HOGENOM; CLU_020120_1_0_5; -.
DR   OMA; IIGINRQ; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF13180; PDZ_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Periplasm; Protease; Repeat; Serine protease; Signal;
KW   Stress response.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..508
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000026934"
FT   DOMAIN          286..377
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          413..497
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          119..284
FT                   /note="Serine protease"
FT   ACT_SITE        134
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        164
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        242
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   BINDING         240..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         297..301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  55599 MW;  D2F53A690ECD0AD7 CRC64;
     MVNLKIVIVI IVLISSNVVL AKENSRSLKV AAQEENEFTE INSAPLKVSE AARYSFADIV
     EPLIPAVVNI STIEYVNSKS ENAEKDPLQE KVNDFLEKLN IPLNLEEVDQ TPKSVPLGSG
     FIIEPNGLIV TNYHVIANVD KINIKLADNT ELSAKLIGND TKTDLALLKI DSEEPLPFVE
     FGDSNDARVG DWVIAIGNPF GNLGGTVTSG IISSKGRDID IDTDNIVDNF IQTDAAINNG
     NSGGPMFNLD QKVIGVNTAI FSPLGTNIGI GFAIPSNTAK PIIERLKKDG KVSRGRLGVT
     IQDLTEDISE GLGLKNTRGV LVAKVQEDGP GDKAGIKTGD IIIEFADIPV KNTKKLRVII
     ADAPIDQEVK VKILRDKKEL ELPIKITSDN EEVTKDSTEE TNKKEITNKE ENNLSITKNN
     ITFGNLTEEL RQKYTIPQDK MGIVITNIDE EESSFKIGDL ITNINQKSID DISKLEELYE
     NAKKSDKKNI LLLIERGSSN MFVPLQVM