ID   H1Q4S2_9BACT            Unreviewed;       860 AA.
AC   H1Q4S2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Spi protease inhibitor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9140_01910 {ECO:0000313|EMBL:EHO66965.1};
OS   Prevotella micans F0438.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=883158 {ECO:0000313|EMBL:EHO66965.1, ECO:0000313|Proteomes:UP000016023};
RN   [1] {ECO:0000313|EMBL:EHO66965.1, ECO:0000313|Proteomes:UP000016023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0438 {ECO:0000313|EMBL:EHO66965.1,
RC   ECO:0000313|Proteomes:UP000016023};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Wade W.G., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella micans F0438.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C10 family.
CC       {ECO:0000256|ARBA:ARBA00009693}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHO66965.1}.
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DR   EMBL; AGWK01000052; EHO66965.1; -; Genomic_DNA.
DR   RefSeq; WP_006953506.1; NZ_JH594523.1.
DR   AlphaFoldDB; H1Q4S2; -.
DR   STRING; 883158.HMPREF9140_01910; -.
DR   MEROPS; C10.004; -.
DR   PATRIC; fig|883158.3.peg.1914; -.
DR   eggNOG; COG3209; Bacteria.
DR   HOGENOM; CLU_336758_0_0_10; -.
DR   Proteomes; UP000016023; Unassembled WGS sequence.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12480; -; 1.
DR   Gene3D; 3.90.70.50; Peptidase C10, streptopain; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR026906; LRR_5.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR041286; MBG_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; PF13306; LRR_5; 2.
DR   Pfam; PF18676; MBG_2; 1.
DR   Pfam; PF01640; Peptidase_C10; 1.
DR   PRINTS; PR00797; STREPTOPAIN.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016023};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..860
FT                   /note="Spi protease inhibitor domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003552973"
FT   DOMAIN          26..113
FT                   /note="Spi protease inhibitor"
FT                   /evidence="ECO:0000259|Pfam:PF13734"
FT   DOMAIN          731..805
FT                   /note="MBG"
FT                   /evidence="ECO:0000259|Pfam:PF18676"
FT   ACT_SITE        180
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600200-1"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600200-1"
SQ   SEQUENCE   860 AA;  94012 MW;  69290139B0FDB5AB CRC64;
     MNYSSKRLST CLVMLFSFIL AITAGPRSKA AIKAAAIKAL ESSSLRMNSI TRGQLKMLQV
     NKEFVVMGYE DGGFVIVSKD DLTPEIIGYS TTDFNEAIKN ESFKWYLKAV QATVESIVAS
     GKSYKTIKPD INKFPAQMSP LIKSHWGQES PYNDLCPEGT VSGTGSWQGY GKTGRTVSGC
     VATAMAQIIY YNRFPSRGNG THSVRVKQAD GSYKTVAVNY DESIYDYDNM LNDYKQGSYN
     AVQGKAVAKL MLDCGVASDM QYATDGSGTY TSNAAVGLRR NFGYPATTRM VERKNFSEED
     WMDMVFTEVS AHRAILYTGV DLANGGHAFV LCGYNSDGKV WINWGWNGSA DGYYDIALLN
     PKSSGLKFSS YQDMIIGFGG KPVDTVKDTV TVASPGTLNT LIPDSLVTRI SLLKVNGNIN
     STDIKFIRLI AGYDDKNKTT HSSLSVLDLS DANIVAGGDA YLIEGDKSLT TVDNVLPERA
     FYNVSGLNKL YLPKTMKSFG NGAFGRLVSL DSLYIPTGAD KEYVVMDKVI YNADTTNVLA
     TYSYREGEIT LPATVTEIND YGMSGASMLT RVNLPASLKF IGNEAFAGNY ALEQIRCYFK
     DPVALGSKVF NEMDKSSIKL YVPAGSLTKF KRAAQWKDFY TVAHKNIIEF GTSLKVRNAL
     RRYGENNPSF GWKTEGDFVN GRPELSCEAT PTSPVGKYVI HISRGTITEP MVDFHDGYLT
     VEKAIAEMKA DDKTIDGDET LQFTYTVSGL KNNETSVVLT VQPQFSIVDA MGQTVTNYSK
     KGTYYISISG AESQNYTFNY TPGTLIVKSS ATGIDNVQSA NSEARFDIYT VSGALIGKGV
     ISLRGLPKGV YIVNGKKIVK
//