ID   DEGP_BUCAI              Reviewed;         478 AA.
AC   P57322;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Probable serine protease do-like;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=degP; OrderedLocusNames=BU228;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR   EMBL; BA000003; BAB12943.1; -; Genomic_DNA.
DR   RefSeq; NP_240057.1; NC_002528.1.
DR   RefSeq; WP_010896016.1; NC_002528.1.
DR   AlphaFoldDB; P57322; -.
DR   SMR; P57322; -.
DR   STRING; 107806.10038908; -.
DR   EnsemblBacteria; BAB12943; BAB12943; BAB12943.
DR   KEGG; buc:BU228; -.
DR   PATRIC; fig|107806.10.peg.241; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_1_6; -.
DR   OMA; EGKGPWP; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; Protease; Reference proteome; Repeat;
KW   Serine protease; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..478
FT                   /note="Probable serine protease do-like"
FT                   /id="PRO_0000026927"
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   DISULFID        87..99
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  52230 MW;  868E8732CAC50629 CRC64;
     MKKSAIILSK IILILTLLLS FGMSWNNVFS NTKNSIVSRE ISPSLAPMLE KVMPSVISIN
     IEGSAITRTS RLPHQFQPFF GDNSPFCQGN SPFRHSPFCH INPDSDDKKE KFRALGSGVI
     INADKGYAVT NNHVVENANK IQVQLSDGRR YEARVIGKDS RSDIALIQLK NANNLSEIKI
     ADSDNLRVGD YTVAIGNPYG LGETVTSGII SALGRSGLNI EHYENFIQTD AAINRGNSGG
     ALVNLKGELI GINTAILAPD GGNIGIGFAI PCNMVKNLTA QMVQFGQVRR GELGIMGMEL
     NSDLAQIMKI NSQKGAFVSR VLPNSSAFEA GIKAGDIIIS LNRKPISSFS SLRAEIGSLP
     VATKMELGVF REGRIKNITV ELKHSVKHNL NSENDYIGIE GVDLSDYIFN EQKVIKVDNV
     KPHTPASKIG FKKDDIILNV NQKLISNVDE LKKFLHSKPK ILVFNIKRGN DTIYLVSE