ID   DEGPL_CHLTR             Reviewed;         497 AA.
AC   P18584; O84830;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like;
DE            EC=3.4.21.107;
DE   AltName: Full=59 kDa immunogenic protein;
DE   AltName: Full=Protease Do;
DE   AltName: Full=SK59;
DE   Flags: Precursor;
GN   Name=htrA; OrderedLocusNames=CT_823;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L2;
RX   PubMed=2379836; DOI=10.1016/0378-1119(90)90439-x;
RA   Kahane S., Weinstein Y., Sarov I.;
RT   "Cloning, characterization and sequence of a novel 59-kDa protein of
RT   Chlamydia trachomatis.";
RL   Gene 90:61-67(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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=AAA23116.1; Type=Miscellaneous discrepancy; Note=Sequencing errors. The putative 59 kDa immunogenic protein was translated on the complementary strand to that of what seems to be the real protein.; Evidence={ECO:0000305};
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DR   EMBL; M31119; AAA23116.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE001273; AAC68420.1; -; Genomic_DNA.
DR   PIR; H71465; H71465.
DR   PIR; JQ0642; JQ0642.
DR   RefSeq; NP_220344.1; NC_000117.1.
DR   RefSeq; WP_009872209.1; NC_000117.1.
DR   AlphaFoldDB; P18584; -.
DR   SMR; P18584; -.
DR   STRING; 813.O172_04600; -.
DR   MEROPS; S01.480; -.
DR   EnsemblBacteria; AAC68420; AAC68420; CT_823.
DR   GeneID; 884623; -.
DR   KEGG; ctr:CT_823; -.
DR   PATRIC; fig|272561.5.peg.909; -.
DR   HOGENOM; CLU_020120_1_0_0; -.
DR   InParanoid; P18584; -.
DR   OMA; IIGINRQ; -.
DR   Proteomes; UP000000431; 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; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
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   Pfam; PF17820; PDZ_6; 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; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Periplasm; Protease; Reference proteome; Repeat;
KW   Serine protease; Signal; Stress response.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..497
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000026932"
FT   DOMAIN          290..381
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          394..485
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          128..289
FT                   /note="Serine protease"
FT   ACT_SITE        143
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        173
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   497 AA;  53244 MW;  86A5E31BB84A38BA CRC64;
     MMKRLLCVLL STSVFSSPML GYSASKKDSK ADICLAVSSG DQEVSQEDLL KEVSRGFSRV
     AAKATPGVVY IENFPKTGNQ AIASPGNKRG FQENPFDYFN DEFFNRFFGL PSHREQQRPQ
     QRDAVRGTGF IVSEDGYVVT NHHVVEDAGK IHVTLHDGQK YTAKIVGLDP KTDLAVIKIQ
     AEKLPFLTFG NSDQLQIGDW AIAIGNPFGL QATVTVGVIS AKGRNQLHIV DFEDFIQTDA
     AINPGNSGGP LLNINGQVIG VNTAIVSGSG GYIGIGFAIP SLMAKRVIDQ LISDGQVTRG
     FLGVTLQPID SELATCYKLE KVYGALVTDV VKGSPAEKAG LRQEDVIVAY NGKEVESLSA
     LRNAISLMMP GTRVVLKIVR EGKTIEIPVT VTQIPTEDGV SALQKMGVRV QNITPEICKK
     LGLAADTRGI LVVAVEAGSP AASAGVAPGQ LILAVNRQRV ASVEELNQVL KNSKGENVLL
     MVSQGDVVRF IVLKSDE