DEGPL_CHLPN
ID DEGPL_CHLPN Reviewed; 488 AA.
AC Q9Z6T0; Q9JQD7; Q9K1W4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
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=CPn_0979, CP_0877, CpB1016;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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=AAP98945.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE001363; AAD19116.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38665.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99186.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98945.1; ALT_INIT; Genomic_DNA.
DR PIR; G72011; G72011.
DR PIR; G81528; G81528.
DR PIR; H86612; H86612.
DR RefSeq; NP_225173.1; NC_000922.1.
DR RefSeq; WP_010883612.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z6T0; -.
DR SMR; Q9Z6T0; -.
DR STRING; 115711.CP_0877; -.
DR EnsemblBacteria; AAD19116; AAD19116; CPn_0979.
DR EnsemblBacteria; AAF38665; AAF38665; CP_0877.
DR KEGG; cpa:CP_0877; -.
DR KEGG; cpj:htrA; -.
DR KEGG; cpn:CPn_0979; -.
DR KEGG; cpt:CpB1016; -.
DR PATRIC; fig|115713.3.peg.1074; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_0; -.
DR OrthoDB; 741829at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..488
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /id="PRO_0000026931"
FT DOMAIN 281..372
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 388..476
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 119..280
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 238
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT BINDING 236..238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 293..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="S -> G (in Ref. 4; AAP98945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 52311 MW; 0EE7E0F88F106F49 CRC64;
MITKQLRSWL AVLVGSSLLA LPLSGQAVGK KESRVSELPQ DVLLKEISGG FSKVATKATP
AVVYIESFPK SQAVTHPSPG RRGPYENPFD YFNDEFFNRF FGLPSQREKP QSKEAVRGTG
FLVSPDGYIV TNNHVVEDTG KIHVTLHDGQ KYPATVIGLD PKTDLAVIKI KSQNLPYLSF
GNSDHLKVGD WAIAIGNPFG LQATVTVGVI SAKGRNQLHI ADFEDFIQTD AAINPGNSGG
PLLNIDGQVI GVNTAIVSGS GGYIGIGFAI PSLMANRIID QLIRDGQVTR GFLGVTLQPI
DAELAACYKL EKVYGALVTD VVKGSPADKA GLKQEDVIIA YNGKEVDSLS MFRNAVSLMN
PDTRIVLKVV REGKVIEIPV TVSQAPKEDG MSALQRVGIR VQNLTPETAK KLGIAPETKG
ILIISVEPGS VAASSGIAPG QLILAVNRQK VSSIEDLNRT LKDSNNENIL LMVSQGDVIR
FIALKPEE
