ID   DEGPL_BUCBP             Reviewed;         465 AA.
AC   Q89AP5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=bbp_210;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26942.1; -; Genomic_DNA.
DR   RefSeq; WP_011091343.1; NC_004545.1.
DR   AlphaFoldDB; Q89AP5; -.
DR   SMR; Q89AP5; -.
DR   STRING; 224915.bbp_210; -.
DR   EnsemblBacteria; AAO26942; AAO26942; bbp_210.
DR   GeneID; 56470752; -.
DR   KEGG; bab:bbp_210; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_1_6; -.
DR   OMA; CKHEAVV; -.
DR   OrthoDB; 741829at2; -.
DR   Proteomes; UP000000601; 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; IPR036034; PDZ_sf.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF00595; PDZ; 2.
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   Disulfide bond; Hydrolase; Periplasm; Protease; Reference proteome; Repeat;
KW   Serine protease; Signal; Stress response.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..465
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000026929"
FT   DOMAIN          268..359
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          365..457
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          102..240
FT                   /note="Serine protease"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        224
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   BINDING         222..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         279..283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        85..91
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  51086 MW;  57B3677C05838E78 CRC64;
     MKKITMIFNT VLIFLVFLLI SGFSWHKSEI PTQEKFFESK SFSLSTVLEK VIPSVVSITV
     EGNVTQSTRI PRQFQSSFNK KVLDCFGISR CMTRQGKFHA LGSGVILDSK NGYIVTNSHV
     VDRANKIQVQ LSNGCKHEAV VIGKDARFDI AIIKLKKVKN LHEIKMSNSD ILKVGDYVIA
     IGNPYGLGET VTSGIISALH RSGLNIENYE NFIQTDAAIN RGNSGGALVN LKGELIGINT
     AILTPDGGNI GIGFAIPINM VNNLTTQILE YGQVKQNELG IVGMELNSDL AKVLKINVHR
     GAFISQVLSK SPADVSGIKP GDVIILLNRK PIASFATLRA EIASFPIKTK IELGILRNKK
     VKFIIVELKQ KIQSKIDSSV LCKLISGASL SNFRIHGQNK GICVNYVNNG TPAYRTGLRK
     NDIIFEVNKY QVSSLSNFQK VLKTKPLILV LHVKRGNDVL YLVTH