ID   A0A1G5QM35_9MICC        Unreviewed;      1058 AA.
AC   A0A1G5QM35;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Peptidase inhibitor I9 {ECO:0000313|EMBL:SCZ62610.1};
GN   ORFNames=SAMN02799638_03459 {ECO:0000313|EMBL:SCZ62610.1};
OS   Arthrobacter sp. UNCCL28.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1502752 {ECO:0000313|EMBL:SCZ62610.1, ECO:0000313|Proteomes:UP000199526};
RN   [1] {ECO:0000313|EMBL:SCZ62610.1, ECO:0000313|Proteomes:UP000199526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNCCL28 {ECO:0000313|EMBL:SCZ62610.1,
RC   ECO:0000313|Proteomes:UP000199526};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FMWE01000006; SCZ62610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5QM35; -.
DR   STRING; 1502752.SAMN02799638_03459; -.
DR   Proteomes; UP000199526; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 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; IPR003137; PA_domain.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
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   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..1058
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011689087"
FT   DOMAIN          97..162
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          192..670
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          475..542
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          724..816
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   REGION          1024..1058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1028..1048
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        302
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        627
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1058 AA;  107900 MW;  5FEC5B3867767BAB CRC64;
     MKSQGKSFVR SGGLRKAAAL AVGLPLLLSS MAMPAQAAPT PETPGNVAGV AKKNLDPSAY
     KDGRYMVVLA EKPAATYDGG TAGLAPTKPE EGKKLDADSA PVKEYQQHLQ TQQQEIASQE
     NITIERDFTT AVNGFSANLS ADQAINLAKD PKVLMVAPDT QYAPDYSTTD FLKLSGPNGT
     WATQYGGQDN AGKGTVVGVI DTGYTPSNPF FAGEPVGPLV GNPQVGVPYR TADGKIAMLK
     ADGDTFIGEC QPGKDTGADY DGSACNSKVL STHYFADAFL ETVAPENRAP EEVISPVDVD
     SHGTHTASTA AGNANVDAVV DGRSFGTTSG IAPAAKLSIY KVCWEDTDPA TGGCYGSASV
     DAIEQAILDG VDVLNYSISG STTSTTDPVS LAFLSAASAG IFVATSAGNS GPTASTVNHG
     APWLTTVAAT SFSQELQGTV EFSDGSKFRG ASIMNREVSG AGVVLSTNAA SGEGNAALCA
     PGSLDPAKVA GKVVVCDRGV VDRTAKSAEV LRGGGVGMIL VNLTDSSLDT DKHVIPTVHV
     NPPATQTIKD KVTANPAITV SLLNRDTTGL PAEAQPQIAG FSSRGPLLAT DSDLLKPDVS
     APGVAILAGV SPIGTGGDNF GFLSGTSMAS PHVAGFGALI LGKNPKWSPA TVKSAMMTTA
     GPVKLANGSV NKDVFATGAG QVDPAKVLSP GLVYDATTED YLKFIQGTGM DLGMEGLGTT
     APRDMNVPSF ALGNLAGKIE VTRTVTALTP GLYRATANVP GVNVKVTPSV LNFGAAGEKK
     TFKVQFENNS AALGKFAMGS LSWQGANKTV TSPIAVRPQS VIADKALAFT GTGPNGSAAI
     NITSGTNLPV GVTVDGLSKA DSSAVELVPG PFAGETNASN YVKKVTVGEG SALAKFSVIS
     SNDAADFDML VLTPSGQQLP AATASASETL SVPNPAAGDY YIFANLYASP NNQATKATVD
     AAVLGANQGN ATVTPNPIRL ANGKTGQISL NWKNLEPGSY IGRLTFAGTS EPSFVTVLVN
     PGGAVVVPDE EDPKKDKKDK KNHGKIRGDE PAQSNNAG
//