ID   A0A143HN66_9GAMM        Unreviewed;       542 AA.
AC   A0A143HN66;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Peptidase inhibitor I9 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A3224_11705 {ECO:0000313|EMBL:AMX03149.1};
OS   Microbulbifer thermotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX03149.1, ECO:0000313|Proteomes:UP000076077};
RN   [1] {ECO:0000313|Proteomes:UP000076077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA   Lee Y.-S., Choi Y.-L.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; CP014864; AMX03149.1; -; Genomic_DNA.
DR   RefSeq; WP_067154782.1; NZ_CP014864.1.
DR   AlphaFoldDB; A0A143HN66; -.
DR   STRING; 252514.A3224_11705; -.
DR   GeneID; 76608709; -.
DR   KEGG; mthd:A3224_11705; -.
DR   Proteomes; UP000076077; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR043708; DUF5648.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF18885; DUF5648; 3.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000076077};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          38..111
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          154..372
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        157
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        343
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   542 AA;  59494 MW;  29D70D13E1ACDEED CRC64;
     MKGNILSRTF LAAILFFIFS KSAISAEIYF SENSETDKYV VVLKDKKNGN RELISKYAGL
     KHSEKAALMA YENRLNIRRV YNEVINGFVV EGDLDSVKEL SKNPEVEYIE QVGKVSISAT
     QYEAVWNLDR IDQRNKNYDG KYTYDRTGSG VNAYIIDTGI RISHSEFEGR AKAGWDFVLN
     QVGDGTDCHG HGTHVAGIVG GKTYGVAKAV TLTALRVLAC DGYGSNDDVI AALEWVIQNG
     KKPGVINMSL GSGASLAVDT AVKNAINAGF AVVAAAGNEA QDACNRSPAR AKEVITVGAT
     DRNDRVAWFS NYGQCLDVWA PGVDIISADS SSDKASILRD GTSMAAPHVT GIAALYLQGS
     PNASANSVIN NIMGKVTYGK LVNIPPEREC PNLLAYSKGT SNTYTAIHRY YNGEVKNHFY
     TKNWSELQSA PTPTWRYEGV IGYAYRKNTE NTKPFYRYYH SGVKDHFYTT NYGELGSGHS
     GWVYEGIAAY LPTSGNTKDI YRYYNSMVKD HFYTTSWGEL EGGNSNWKYE GIAGKIFAGP
     QD
//