PTP_PORGI
ID PTP_PORGI Reviewed; 732 AA.
AC Q7MUW6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Prolyl tripeptidyl peptidase {ECO:0000303|PubMed:10092598};
DE Short=PTP {ECO:0000303|PubMed:18042490};
DE EC=3.4.14.12;
DE AltName: Full=Prolyl tripeptidyl peptidase 81.8 kDa form {ECO:0000303|PubMed:10092598};
DE AltName: Full=Prolyl tripeptidyl peptidase A {ECO:0000303|PubMed:10092598};
DE Contains:
DE RecName: Full=Prolyl tripeptidyl peptidase 75.8 kDa form {ECO:0000303|PubMed:10092598};
DE Flags: Precursor;
GN Name=ptpA {ECO:0000303|PubMed:10092598}; OrderedLocusNames=PG_1361;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 81-97; 113-126 AND 597-612, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND BLOCKAGE
RP OF N-TERMINUS.
RX PubMed=10092598; DOI=10.1074/jbc.274.14.9246;
RA Banbula A., Mak P., Bugno M., Silberring J., Dubin A., Nelson D.,
RA Travis J., Potempa J.;
RT "Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme
RT with possible pathological implications for the development of
RT periodontitis.";
RL J. Biol. Chem. 274:9246-9252(1999).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 39-732.
RX PubMed=16914159; DOI=10.1016/j.jmb.2006.06.083;
RA Ito K., Nakajima Y., Xu Y., Yamada N., Onohara Y., Ito T., Matsubara F.,
RA Kabashima T., Nakayama K., Yoshimoto T.;
RT "Crystal structure and mechanism of tripeptidyl activity of prolyl
RT tripeptidyl aminopeptidase from Porphyromonas gingivalis.";
RL J. Mol. Biol. 362:228-240(2006).
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 39-732 IN COMPLEX WITH INHIBITOR,
RP AND MUTAGENESIS OF GLU-205 AND GLU-636.
RX PubMed=18042490; DOI=10.1016/j.jmb.2007.09.077;
RA Xu Y., Nakajima Y., Ito K., Zheng H., Oyama H., Heiser U., Hoffmann T.,
RA Gartner U.T., Demuth H.U., Yoshimoto T.;
RT "Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas
RT gingivalis and details of substrate-recognition mechanism.";
RL J. Mol. Biol. 375:708-719(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.
CC {ECO:0000269|PubMed:10092598}.
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:0000269|PubMed:10092598};
CC -!- ACTIVITY REGULATION: Strongly inhibited by diisopropyl fluorophosphate
CC and Pefabloc. Weakly inhibited by 3,4-dichloroisocumarin. Not inhibited
CC by phenylmethylsulfonyl fluoride, leupeptin, antipain or prolinal.
CC Activated by iodoacetamide. {ECO:0000269|PubMed:10092598}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|PubMed:10092598};
CC Temperature dependence:
CC Stable for at least 12 hours at 25 or 37 degrees Celsius (at pH 7.6).
CC {ECO:0000269|PubMed:10092598};
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10092598}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000255}.
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DR EMBL; AE015924; AAQ66425.1; -; Genomic_DNA.
DR RefSeq; WP_005873421.1; NC_002950.2.
DR PDB; 2D5L; X-ray; 2.10 A; A=39-732.
DR PDB; 2DCM; X-ray; 2.90 A; A=39-732.
DR PDB; 2EEP; X-ray; 2.20 A; A=39-732.
DR PDB; 2Z3W; X-ray; 2.00 A; A=39-732.
DR PDB; 2Z3Z; X-ray; 1.95 A; A=39-732.
DR PDBsum; 2D5L; -.
DR PDBsum; 2DCM; -.
DR PDBsum; 2EEP; -.
DR PDBsum; 2Z3W; -.
DR PDBsum; 2Z3Z; -.
DR AlphaFoldDB; Q7MUW6; -.
DR SMR; Q7MUW6; -.
DR STRING; 242619.PG_1361; -.
DR DrugBank; DB07813; GLYCYLALANYL-N-2-NAPHTHYL-L-PROLINEAMIDE.
DR ESTHER; porgi-q7muw6; DPP4N_Peptidase_S9.
DR MEROPS; S09.017; -.
DR EnsemblBacteria; AAQ66425; AAQ66425; PG_1361.
DR KEGG; pgi:PG_1361; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_006105_2_0_10; -.
DR OMA; MYGERYM; -.
DR OrthoDB; 821953at2; -.
DR BRENDA; 3.4.14.12; 756.
DR EvolutionaryTrace; Q7MUW6; -.
DR Proteomes; UP000000588; 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 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Direct protein sequencing; Hydrolase;
KW Protease; Reference proteome; 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_0000394757"
FT CHAIN 81..732
FT /note="Prolyl tripeptidyl peptidase 75.8 kDa form"
FT /evidence="ECO:0000269|PubMed:10092598"
FT /id="PRO_0000394758"
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"
FT MUTAGEN 205
FT /note="E->Q: Inactive."
FT /evidence="ECO:0000269|PubMed:18042490"
FT MUTAGEN 636
FT /note="E->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18042490"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2DCM"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 393..403
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 491..500
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 537..543
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 561..565
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 573..587
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 592..602
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 604..615
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 620..627
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 637..644
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 651..657
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 659..665
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 668..675
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT HELIX 684..696
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:2Z3Z"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:2Z3W"
FT HELIX 716..731
FT /evidence="ECO:0007829|PDB:2Z3Z"
SQ SEQUENCE 732 AA; 82266 MW; FE08469EB5562810 CRC64;
MKKTIFQQLF LSVCALTVAL PCSAQSPETS GKEFTLEQLM PGGKEFYNFY PEYVVGLQWM
GDNYVFIEGD DLVFNKANGK SAQTTRFSAA DLNALMPEGC KFQTTDAFPS FRTLDAGRGL
VVLFTQGGLV GFDMLARKVT YLFDTNEETA SLDFSPVGDR VAYVRNHNLY IARGGKLGEG
MSRAIAVTID GTETLVYGQA 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 KGSHTLLEAK 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
