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Database: UniProt
Entry: A0A022MHE1_9ACTN
LinkDB: A0A022MHE1_9ACTN
Original site: A0A022MHE1_9ACTN 
ID   A0A022MHE1_9ACTN        Unreviewed;       533 AA.
AC   A0A022MHE1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:EYT81957.1};
GN   ORFNames=CF54_16275 {ECO:0000313|EMBL:EYT81957.1};
OS   Streptomyces sp. Tu 6176.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT81957.1, ECO:0000313|Proteomes:UP000020060};
RN   [1] {ECO:0000313|EMBL:EYT81957.1, ECO:0000313|Proteomes:UP000020060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT81957.1,
RC   ECO:0000313|Proteomes:UP000020060};
RA   Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT   "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT   cytotoxic benzoxazol nataxazol.";
RL   Submitted (MAR-2014) 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}.
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:EYT81957.1}.
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DR   EMBL; JFJQ01000508; EYT81957.1; -; Genomic_DNA.
DR   RefSeq; WP_018567277.1; NZ_KK106989.1.
DR   AlphaFoldDB; A0A022MHE1; -.
DR   HOGENOM; CLU_011263_1_7_11; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000020060; 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; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-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; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
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; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..533
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001502666"
FT   DOMAIN          415..533
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          392..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        165
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        198
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        358
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   533 AA;  54631 MW;  86FC0096F9144FCA CRC64;
     MEFDARAVRR VLAAGASAAL LFGAAITQAT AAPVPPGGGE GRIVGADRPG AVDGSYIVTF
     KNSVDRADVP ASAKALVARH AGSLRYTYTA ALHGFAARMS PQEAKKLAAD PSVARVEADA
     AAYAVDTQTN PPSWGLDRVD QRDLPVDRSY TYGSTASNVN AYIVDTGVRL SHRDFGGRAV
     SGYDFIDNDT NASDCAGHGT HVAGTVGGGS YGVAKGVKLV SVRVLNCQGT SGDTWAPVLA
     GIDWVTKNAV KPAVANMSIG GGRTQSVNDA VAASIASGVT WVVAAGNNNA DACSYSPAST
     ASAITVGATD SRDARATGWS NGQGSNYGSC LDIFAPGDSI VSSSNAGDTA SQTMSGTSMA
     TPHVAGAAAL LLAAHPTWSP AQVRDRLVAD ATSGKVTDPR TGSPNKLLYT GTGTTTPPTG
     TTFENTDDYT IRDNSTVESP LAVTGVSGNA PAALSVHVDI RHTFRGDLKV ELVAPNGTAH
     LLKNFDSNDS ADNVQATYTV DASAAPANGT WKLRVTDNWA NDTGYINAWS LQF
//
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