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Database: UniProt
Entry: A0A1C6UND4_9ACTN
LinkDB: A0A1C6UND4_9ACTN
Original site: A0A1C6UND4_9ACTN 
ID   A0A1C6UND4_9ACTN        Unreviewed;       405 AA.
AC   A0A1C6UND4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:SCL55423.1};
GN   ORFNames=GA0070603_2004 {ECO:0000313|EMBL:SCL55423.1};
OS   Micromonospora chersina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL55423.1, ECO:0000313|Proteomes:UP000198605};
RN   [1] {ECO:0000313|EMBL:SCL55423.1, ECO:0000313|Proteomes:UP000198605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL55423.1,
RC   ECO:0000313|Proteomes:UP000198605};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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; FMIB01000002; SCL55423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6UND4; -.
DR   STRING; 47854.GA0070603_2004; -.
DR   OrthoDB; 9766923at2; -.
DR   Proteomes; UP000198605; 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; cd07477; Peptidases_S8_Subtilisin_subset; 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; 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   InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..405
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008747881"
FT   DOMAIN          34..98
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          130..380
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        136
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        168
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        348
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   405 AA;  40512 MW;  DE101D7BBE779FF1 CRC64;
     MRKTLGVAML TGIVVAASAT GATAAPRAEA ESGYIVVLRA GANPSSVAAE QSRATGATVG
     HVYEHALRGY SARMSATAAA RLARDSRVLL VQPDGVVTAD AQTTPTGINR ADAELSPTAK
     INGADERVNV DVAVIDTGID LTHPDLNVYT AGAKNCSTGS SANDGNGHGS HVAGTIGALD
     NGVGVVGMAP GARLWPVRVL NNAGSGSFSS IICGIDYVTA HASEIEVANM SLGGSGSDSA
     CGSNKDAMHE AICNSVVAGV TYVVAAGNET DNAANHVPAA YDEVITVSAL ADFNGLPGGG
     AAATCRSDVD DTIADFSNYG ADVDLMAPGV CIYSTWKGGG YNTISGTSMA SPHVAGGAAL
     YKATHPTATP GAVKSALQSA GTTNYSWPAG DPDGIQEKLL NVATF
//
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