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 27-MAR-2024, entry version 119.
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; Pseudomonadota; 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 KEGG; bab:bbp_210; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_6; -.
DR OrthoDB; 9758917at2; -.
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 CDD; cd00987; PDZ_serine_protease; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
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 NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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
//
