ID   PRTT_PORGN              Reviewed;         868 AA.
AC   P43158;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Thiol protease/hemagglutinin PrtT;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=prtT;
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 53977;
RX   PubMed=8093357; DOI=10.1128/iai.61.1.117-123.1993;
RA   Otogoto J., Kuramitsu H.K.;
RT   "Isolation and characterization of the Porphyromonas gingivalis prtT gene,
RT   coding for protease activity.";
RL   Infect. Immun. 61:117-123(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC   STRAIN=ATCC 53977;
RX   PubMed=7806362; DOI=10.1128/iai.63.1.238-247.1995;
RA   Madden T.E., Clark V.L., Kuramitsu H.K.;
RT   "Revised sequence of the Porphyromonas gingivalis prtT cysteine
RT   protease/hemagglutinin gene: homology with streptococcal pyrogenic exotoxin
RT   B/streptococcal proteinase.";
RL   Infect. Immun. 63:238-247(1995).
CC   -!- FUNCTION: Appears to be specific for arginine-containing peptide bonds.
CC       Possesses hemagglutinin activity.
CC   -!- SIMILARITY: Belongs to the peptidase C10 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; M83096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   MEROPS; C10.002; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.50; -; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000200; Peptidase_C10.
DR   InterPro; IPR025896; Spi_Prtas-inh.
DR   InterPro; IPR044934; Streptopain_sf.
DR   Pfam; PF13734; Inhibitor_I69; 1.
DR   Pfam; PF01640; Peptidase_C10; 1.
DR   PRINTS; PR00797; STREPTOPAIN.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Hemagglutinin; Hydrolase; Protease; Signal; Thiol protease.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028501"
FT   CHAIN           ?..868
FT                   /note="Thiol protease/hemagglutinin PrtT"
FT                   /id="PRO_0000028502"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   868 AA;  96445 MW;  45436EFE32779323 CRC64;
     MKRIFYTLGL LLLCLPMLQA GPVTRSKAEQ TAKNFFAKRQ PTLSSSTASL RMDFVYKAAE
     REEALFFVFN RGEKDGFLLV AADDRFPEVI GYAFKGHFDA ARMPDNLRGW LKGYEREMLA
     VMDGKAEPID PIREAKPTRD LPSSIAPILE TGEHASDPIL WDQGYPFNTL HPLLPSGQQA
     YTGCVATAMG QIMRHYKWPE KASGEYDYYD DMTGTHTHYS GTFGETYNWS KMPGNISVGI
     SPEEVKALST FMRDVSFSVN MQFADFGSGT FSIFVERALR ETFHYKKSLR YIHRSLLPGK
     EWKDMIRKEL AENRPVYYAG ADGSMGHAFV CDGYEPDGTF HFNWGWGGMS NGNFYLNLLN
     PGSLGTGAGD GGYSTDQEVV IGIEPASNEA PGIVPDPTIT LYGLQHNMSD EALDLSVKIK
     NYSTYAGDVK LAYRLTLPNG TETTNPAVTV PIVWEDIIGE STGNITIPCS QFAEGKNTIS
     ILYRTDGMAD WKELKHILMG LVNKIEVTMP AGDVAYSVAD ARIVLKDGSL SHNLKAYSDC
     KLSATVYNPG TEEFRSRVTF ALRNTEGRLY FLGRHLVELH PGDEDGEKVS LTITGLKARA
     GQYMLVCTGD MELLMEDASW IELASIEVAE HTSTHSSLLV ASNPQIDLLT VHRANPETLP
     TFSITNEGGA TFSGKIEIVA IKAFSETFFQ AKEEHMSLAQ GETKVLSPEL TANSSLYTNA
     ELFPDGIYYI VIREQGFWDP IDLFGDYYYR IRLITDLSSS XIAGKDVSTI VLYPNPAHDY
     VHVAIPPTYA GSTLRLFDIQ GRMQLSTKIR ICRYASRRRT SSEGHLYRCG RRHGREALYS
     LIQSVNSKTD KGNAGWEIPS GHCPCTVC