ID   DEGPL_RICPR             Reviewed;         513 AA.
AC   O05942;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   03-AUG-2022, entry version 129.
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=RP124;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-513.
RC   STRAIN=Madrid E;
RX   PubMed=9274032; DOI=10.1099/00221287-143-8-2783;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genomic rearrangements during evolution of the obligate intracellular
RT   parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp
RT   nucleotide sequence.";
RL   Microbiology 143:2783-2795(1997).
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}.
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DR   EMBL; AJ235270; CAA14593.1; -; Genomic_DNA.
DR   EMBL; Y11782; CAA72471.1; -; Genomic_DNA.
DR   PIR; B71722; B71722.
DR   RefSeq; NP_220516.1; NC_000963.1.
DR   RefSeq; WP_004599755.1; NC_000963.1.
DR   AlphaFoldDB; O05942; -.
DR   SMR; O05942; -.
DR   STRING; 272947.RP124; -.
DR   EnsemblBacteria; CAA14593; CAA14593; CAA14593.
DR   GeneID; 57569252; -.
DR   KEGG; rpr:RP124; -.
DR   PATRIC; fig|272947.5.peg.126; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_5; -.
DR   OMA; IIGINRQ; -.
DR   Proteomes; UP000002480; 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; 1.
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; Reference proteome; Repeat;
KW   Serine protease; Signal; Stress response.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..513
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000026935"
FT   DOMAIN          290..381
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          418..502
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          124..289
FT                   /note="Serine protease"
FT   ACT_SITE        139
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        247
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   BINDING         245..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         302..306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   513 AA;  56310 MW;  4B7E9B7AB4079139 CRC64;
     MVNLKIFLIV IVLMFNNIIL AKENSNALKV VDQEENEFTA INSAPLKISE AARYSFADIV
     EPLIPAVVNI STIEYVNDKS ENSEKDLLQE NKHLGFMSDV LEKLNIPLNL EEIAKTPKSI
     PLGSGFIIAP NGLIVTNYHV IANVEKINIK LADNTEFLAK LIGSDSKTDL ALLKIDSEEP
     LPFVEFGDSN DARVGDWVIA IGNPFGNLGG TVTSGIISSK GRDIDVDTDN IVDNFIQTDA
     AINNGNSGGP MFNLDQKVIG VNTAIFSPLG TNIGIGFAIP SNTAKPIIER LKKDGKVSRG
     RLGVTIQDLT EEISEVLGFK GTNGVLVSKV QENGPGYKAG IKKGDIIIKF GDRLVKNTKK
     LRVIIADTPI NQEVKLKILR DAQELELPIK VTADNEEVIN DSTEETNKAV IINKKENNLS
     ITKNNITFSN LTEELRKKYD IPQDKTGIVI INIDEEESVF KLGDLITNIN HDSIDDIRKL
     EVLYENAKKL EKQNILLLIE RGDTSVFIPL SVS