ID   DEGPL_CHLMU             Reviewed;         497 AA.
AC   Q9PL97;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=TC_0210;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39082.1; -; Genomic_DNA.
DR   PIR; B81728; B81728.
DR   RefSeq; WP_010229828.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PL97; -.
DR   SMR; Q9PL97; -.
DR   STRING; 243161.TC_0210; -.
DR   MEROPS; S01.480; -.
DR   EnsemblBacteria; AAF39082; AAF39082; TC_0210.
DR   GeneID; 1246336; -.
DR   KEGG; cmu:TC_0210; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_0; -.
DR   OMA; IIGINRQ; -.
DR   OrthoDB; 741829at2; -.
DR   Proteomes; UP000000800; 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; Repeat; Serine protease; Signal;
KW   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_0000026930"
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;  53294 MW;  B765F350ACC66BBF CRC64;
     MMKRLLCVLL STSVFSSPML GYSAPKKDSS TGICLAASQS DRELSQEDLL KEVSRGFSKV
     AAQATPGVVY IENFPKTGSQ AIASPGNKRG FQENPFDYFN DEFFNRFFGL PSHREQPRPQ
     QRDAVRGTGF IVSEDGYVVT NHHVVEDAGK IHVTLHDGQK YTAKIIGLDP KTDLAVIKIQ
     AKNLPFLTFG NSDQLQIGDW SIAIGNPFGL QATVTVGVIS AKGRNQLHIV DFEDFIQTDA
     AINPGNSGGP LLNIDGQVIG VNTAIVSGSG GYIGIGFAIP SLMAKRVIDQ LISDGQVTRG
     FLGVTLQPID SELAACYKLE KVYGALITDV VKGSPAEKAG LRQEDVIVAY NGKEVESLSA
     LRNAISLMMP GTRVVLKVVR EGKFIEIPVT VTQIPAEDGV SALQKMGVRV QNLTPEICKK
     LGLASDTRGI FVVSVEAGSP AASAGVVPGQ LILAVNRQRV SSVEELNQVL KNAKGENVLL
     MVSQGEVIRF VVLKSDE