ID   DEGPL_BUCAP             Reviewed;         478 AA.
AC   O85291;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
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=BUsg_222;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9688822; DOI=10.1007/s002849900365;
RA   Thao M.L., Baumann P.;
RT   "Sequence analysis of a DNA fragment from Buchnera aphidicola (Aphid
RT   endosymbiont) containing the genes dapD-htrA-ilvI-ilvH-ftsL-ftsI-murE.";
RL   Curr. Microbiol. 37:214-216(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AF060492; AAC32331.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67781.1; -; Genomic_DNA.
DR   RefSeq; WP_011053748.1; NC_004061.1.
DR   AlphaFoldDB; O85291; -.
DR   SMR; O85291; -.
DR   STRING; 198804.BUsg_222; -.
DR   EnsemblBacteria; AAM67781; AAM67781; BUsg_222.
DR   KEGG; bas:BUsg_222; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_1_6; -.
DR   OMA; EGKGPWP; -.
DR   OrthoDB; 741829at2; -.
DR   Proteomes; UP000000416; 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; 1.
DR   Pfam; PF13180; PDZ_2; 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; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Periplasm; Protease; Repeat; Serine protease;
KW   Signal; Stress response.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..478
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000026928"
FT   DOMAIN          281..372
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          387..469
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          116..254
FT                   /note="Serine protease"
FT   ACT_SITE        133
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        163
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   DISULFID        87..99
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  51303 MW;  C044824F7EF4E98E CRC64;
     MKRINIVLSG IMLFLTLLLS FGMSWGNKNF TSSQNVSSVQ LAPSLAPMLE KVMPSVISIN
     IEGSTVVHTS RLPHQFQPFF GHNSPFCQGN SPFRNSPFCR SNPNSNSMHE KFHALGSGVI
     INADKAYAVT NNHVVENANK IQVQLSDGRR YEASIIGKDS RSDIALIQLK NAKNLSAIKI
     ADSDTLRVGD YTVAIGNPYG LGETVTSGII SALGRSGLNI EHYENFIQTD AAINRGNSGG
     ALVNLKGELI GINTAILAPD GGNIGIGFAI PGNMVKNLTE QMVKFGQVKR GELGIIGMEL
     NSDLAHVMKI NAQKGAFVSQ VLPNSSAFHA GIKAGDIIVS LNKKTISSFA ALRAEVGSLP
     VSTKMELGIF RNGITKNVIV ELKPSLKNSV SLGDIYTGIE GADLSDCSLN GQKGVKIENI
     KLNTQASKIG FKKDDIIVEV NQKVINNLND LKNILDSKPN ILVFSVKRGN NSIYLVSE