ID   PTP_PORG3               Reviewed;         732 AA.
AC   B2RJX3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Prolyl tripeptidyl peptidase {ECO:0000250|UniProtKB:Q7MUW6};
DE            Short=PTP {ECO:0000250|UniProtKB:Q7MUW6};
DE            EC=3.4.14.12;
DE   AltName: Full=Prolyl tripeptidyl peptidase A {ECO:0000250|UniProtKB:Q7MUW6};
DE   Flags: Precursor;
GN   Name=ptpA {ECO:0000250|UniProtKB:Q7MUW6}; OrderedLocusNames=PGN_1149;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
CC   -!- FUNCTION: Serine proteinase. Releases tripeptides from the free amino
CC       terminus of proteins. Has a requirement for Pro in the P1 position, but
CC       is inactivated by Pro in the P1' position (By similarity).
CC       {ECO:0000250|UniProtKB:Q7MUW6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal
CC         tripeptide of a peptide with Pro as the third residue (position P1)
CC         and where Yaa is not proline.; EC=3.4.14.12;
CC         Evidence={ECO:0000250|UniProtKB:Q7MUW6};
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000255}.
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DR   EMBL; AP009380; BAG33668.1; -; Genomic_DNA.
DR   RefSeq; WP_012458062.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RJX3; -.
DR   SMR; B2RJX3; -.
DR   STRING; 431947.PGN_1149; -.
DR   ESTHER; porgi-q7muw6; DPP4N_Peptidase_S9.
DR   MEROPS; S09.017; -.
DR   PRIDE; B2RJX3; -.
DR   EnsemblBacteria; BAG33668; BAG33668; PGN_1149.
DR   GeneID; 29256355; -.
DR   KEGG; pgn:PGN_1149; -.
DR   eggNOG; COG0823; Bacteria.
DR   eggNOG; COG1506; Bacteria.
DR   HOGENOM; CLU_006105_2_0_10; -.
DR   OMA; MYGERYM; -.
DR   BioCyc; PGIN431947:G1G2V-1314-MON; -.
DR   Proteomes; UP000008842; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease; Serine protease; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..732
FT                   /note="Prolyl tripeptidyl peptidase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000394759"
FT   ACT_SITE        603
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   ACT_SITE        678
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   ACT_SITE        710
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
SQ   SEQUENCE   732 AA;  82376 MW;  AE1162049B59CD27 CRC64;
     MKKTIFQQLF LSVCALTVAL PCSAQSPETS GKEFTLEQLM PGGKEFYNFY PEYVVGLQWM
     GDNYVFIEGD DLVFNKANGK SAQTTRFSAA DLNALMPEGC KFQTTDAFPS FRTLDAGRGQ
     VVLFTQRGLV GFDMLARKVT YLFDTNEETA SLDFSPVGDR VAYVRNHNLY IARGGKLGEG
     MSRAIAVTID GAETLVYGQA VHQREFGIEK GTFWSPKGSC LAFYRMDQSM VKPTPIVDYH
     PLEAESKPLY YPMAGTPSHH VTVGIYHLAT GKTVYLQTGE PKEKFLTNLS WSPDENILYV
     AEVNRAQNEC KVNAYDAETG RFVRTLFVET DKHYVEPLHP LTFLPGSNNQ FIWQSRRDGW
     NHLYLYDTTG RLIRQVTKGE WEVTNFAGFD PKGTRLYFES TEASPLERHF YCIDIKGGKT
     KDLTPESGMH RTQLSPDGSA IIDIFQSPTV PRKVTVTNIG KGSYTLLEAK NPDTGYAMPE
     IRTGTIMAAD GQTPLYYKLT MPLHFDPAKK YPVIVYVYGG PHAQLVTKTW RSSVGGWDIY
     MAQKGYAVFT VDSRGSANRG AAFEQVIHRR LGQTEMADQM CGVDFLKSQS WVDADRIGVH
     GWSYGGFMTT NLMLTHGDVF KVGVAGGPVI DWNRYEIMYG ERYFDAPQEN PEGYDAANLL
     KRAGDLKGRL MLIHGAIDPV VVWQHSLLFL DACVKARTYP DYYVYPSHEH NVMGPDRVHL
     YETITRYFTD HL