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Database: UniProt
Entry: A0A0K2RIL7_9MICC
LinkDB: A0A0K2RIL7_9MICC
Original site: A0A0K2RIL7_9MICC 
ID   A0A0K2RIL7_9MICC        Unreviewed;       641 AA.
AC   A0A0K2RIL7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Subtilisin-like protease {ECO:0000313|EMBL:BAS14644.1};
GN   ORFNames=AHiyo8_29470 {ECO:0000313|EMBL:BAS14644.1};
OS   Arthrobacter sp. Hiyo8.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1588023 {ECO:0000313|EMBL:BAS14644.1, ECO:0000313|Proteomes:UP000060353};
RN   [1] {ECO:0000313|Proteomes:UP000060353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hiyo8 {ECO:0000313|Proteomes:UP000060353};
RA   Hiraoka S., Machiyama A., Iwasaki W.;
RT   "Microbial genome analysis of tsunami-affected soil.";
RL   Submitted (FEB-2015) 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; AP014719; BAS14644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K2RIL7; -.
DR   STRING; 1588023.AHiyo8_29470; -.
DR   KEGG; arh:AHiyo8_29470; -.
DR   PATRIC; fig|1588023.3.peg.3073; -.
DR   Proteomes; UP000060353; Chromosome.
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; 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; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 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.
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..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..641
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005482893"
FT   DOMAIN          68..163
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          195..442
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          478..550
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   REGION          573..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        305
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        455
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   641 AA;  65881 MW;  6710ED11BB4610E1 CRC64;
     MNSQGKSFIG SGGLRKAAAL AVGLPVLLSS VALTPAQAAP ASGSTVLGST AAGVARNVDP
     KSYQDGRYVV VLAEKPAATY DGGTPGYVPT KPQAGKKLDV GKAEVKQYQA HLQQKQQDVA
     KQQSVTINRD YTTAINGFSA TLSANQAVNL AKNPDVLLVA PDTQSAPDYS TTDFLNLSGP
     NGAWNTQFGG QDQAGKGTVV GVIDTGYTPT SKFFAGDPVQ PLVGDPQVGI PYRTSDGKIA
     MLKANGDTFV GECQKGTDTG AAFDGTACNS KVLAAHYFAD AFLQTVPPAQ RAPQEQISPI
     DVVSHGTHTA STAAGNPGVE TFVDGRSFGK TSGVAPAAKL SIYKVCWEDT DPNTGGCYSS
     AAIAAIDQAI ADGVDVLNYS ISGATDTTTD PVSLAFLSAA SAGIFVAASA GNSGPQASTV
     NHGAPWMTTV AATSFSQELQ GTVEFSDGTK FRGASIMNHQ VSGAGVVLSA NAASGAGNAA
     LCAPGSLDPA KIAGKVVVCD RGVVDRVAKS AEVLRGGGVG MILVNLTSSS LDTDKHAVPT
     VHVNPPASQA IKDKVGANRH LLFPWLTTTP LGFRSRPSRR SPDSPPAARS SPPIRISSSR
     TSRLPALRCS RVFRRSAAKV MSTDSCPVPP WRPRTLQVSE P
//
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