ID   PRTH_PORGI              Reviewed;         989 AA.
AC   P46071;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Protease PrtH;
DE            EC=3.4.22.-;
GN   Name=prtH;
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 [GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=7927685; DOI=10.1128/iai.62.10.4279-4286.1994;
RA   Fletcher H.M., Schenkein H.A., Macrina F.L.;
RT   "Cloning and characterization of a new protease gene (prtH) from
RT   Porphyromonas gingivalis.";
RL   Infect. Immun. 62:4279-4286(1994).
RN   [2]
RP   ERRATUM OF PUBMED:7927685.
RA   Fletcher H.M., Schenkein H.A., Macrina F.L.;
RL   Infect. Immun. 62:5707-5707(1994).
CC   -!- FUNCTION: Cleaves human complement component C3. May enable
CC       P.gingivalis to evade complement-mediated killing during the immune
CC       response. Plays an important role in soft tissue infections and is a
CC       virulence factor.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=In membrane vesicles.
CC   -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000305}.
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DR   EMBL; L27483; AAA51298.1; -; Genomic_DNA.
DR   AlphaFoldDB; P46071; -.
DR   SMR; P46071; -.
DR   STRING; 242619.PG_2024; -.
DR   MEROPS; C25.001; -.
DR   PRIDE; P46071; -.
DR   eggNOG; COG1974; Bacteria.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR011628; Cleaved_adhesin.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR018832; Pept_C25_gingipain_C.
DR   Pfam; PF07675; Cleaved_Adhesin; 1.
DR   Pfam; PF10365; DUF2436; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Hydrolase; Protease; Repeat; Thiol protease;
KW   Virulence.
FT   CHAIN           1..989
FT                   /note="Protease PrtH"
FT                   /id="PRO_0000216898"
FT   REPEAT          270..323
FT   REPEAT          528..581
FT   REGION          969..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   989 AA;  110238 MW;  FA85FE8A3AC8944C CRC64;
     MHPSTMRCMH LRPVTMHPTS RMLCWKRRLR PKGVRSPEAI RGRIQGTWRQ KTVDLPAGTE
     ICCFPSLPKA PICSTSTLMR LRSKTNAKRA DFTETFESST HGEAPAEWTT IDADGDGQGW
     LCLSSGQLDW LTAHGGTNVV SSFSWNGMAL NPDNYLISKD VTGATKVKYY YAVNDGFPGD
     HYAVMISKTG TNAGDFTVVF EETPNGINKG GARFGLSTEA DGAKPQSVWI ERTVDLPAGT
     KYVAFRHYNC SDLNYILLDD IQFTMGGSPT PTDYTYTVYR DGTKIKEGLT ETTFEEDGVA
     TGNHEYCVEV KYTAGVSPKK CVNVTVNSTQ FNPVKNLKAQ PDGGDVVLKW EAPSAKKTEG
     SREVKRIGDG LFVTIEPAND VRANEAKVVL AADNVWGDNT GYQFLLDADH NTFGSVIPAT
     GPLFTGTASS DLYSANFEYL IPANADPVVT TQNIIVTGQG EVVIPGGVYD YCITNPEPAS
     GKMWIAGDGG NQPARYDDFT FEAGKKYTFT MRRAGMGDGT DMEVEDDSPA SYTYTVYRDG
     TKIKEGLTET TYRDAGLSAQ SHEYCVEVKY TAGVSPKVCV DYIPDGVEDV TVQKPHTLTV
     VGKTITVSWQ GEAMIYDMNG RRLAAGRNTV VYTAQGGYYA VMVVVDGKSY VEETRYQVNL
     SWTRRLCADT SKHRSVIVSE YESVARPPFK EVGRLRFYAY YSNILLKQFV PKSCMKRLSY
     YLPHCKKGSF LRFPRSSTVI TVCQFSWLEY LPVTQGVAGS SPVHTAKIRS CVEIVFRHSS
     IFVCYRSTGK YNYRMRLFNM LGKNFLRTKQ KCLSLLRSAW DIGIKLVLFQ EGRYMESPGQ
     SDEERRTTID FYGNGRYLLF RHSELLVENG YQVKAVVTML GTKPMGRGHK VSPSMVKLYA
     QELGLPILQP DNLNEESFLD ELRTYQPHLQ IVVAFRMLPR SVWQMPPMGT INLHGSLLPM
     YRGAAPIQPR DTPWRYGKRE LPPSASGMR