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Database: UniProt
Entry: A0A0F2CAY5_9MICO
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Original site: A0A0F2CAY5_9MICO 
ID   A0A0F2CAY5_9MICO        Unreviewed;       607 AA.
AC   A0A0F2CAY5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Extracellular serine proteinase {ECO:0000313|EMBL:KJQ54441.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:KJQ54441.1};
GN   ORFNames=RS85_01593 {ECO:0000313|EMBL:KJQ54441.1};
OS   Microbacterium sp. SA39.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ54441.1, ECO:0000313|Proteomes:UP000033425};
RN   [1] {ECO:0000313|EMBL:KJQ54441.1, ECO:0000313|Proteomes:UP000033425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA39 {ECO:0000313|EMBL:KJQ54441.1,
RC   ECO:0000313|Proteomes:UP000033425};
RA   Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (JAN-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,
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:KJQ54441.1}.
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DR   EMBL; JXRU01000032; KJQ54441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2CAY5; -.
DR   STRING; 1263625.RS85_01593; -.
DR   PATRIC; fig|1263625.4.peg.1601; -.
DR   Proteomes; UP000033425; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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; PF05345; He_PIG; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
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:UP000033425};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..607
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002451909"
FT   DOMAIN          53..120
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          154..392
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        163
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        351
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   607 AA;  61473 MW;  D65CED6BC9DF8FA2 CRC64;
     MAPRGLAAAA AALTCASLIM LPSFASANTD STDSPDAPTI IGAESEAAVD GEYLVVLKPQ
     SDLGAADDIA SALTEAVGGE VVEVFNTVID GYSAKLSEDE ALAIASDDRV DHVEQAQMVY
     ALGEQTDPPS WGTDRVDQRG QPLNQRFAYP DSAGAGVNVY VVDSGIRLTH SEFAGRLRPG
     FDAITPGGNA SDCNGHGTHV AGTAVGSTYG IAKKATVYPV RVLDCKGESL STTILTGIEW
     VAENAVRPAT INYSVGCRQA CSIPSIDAAV KSIVASGITW VSAAGNSNDD ACRYSPQLVP
     ETITVGNSTR TDSKAPSSSW GRCLDVWAPG SEIISSWFTG DTEARSATGT SMAAPHVTGA
     TALYLSANPS ATPAQVHAAV VDNATPGTLT GLDTASPNRL LYTGFLNRTT NPAPTAVDLA
     AIANKTGTVG QPLSVSVSAT GGTAPYSFSA TGLPAGLAID AKTGTISGTP TAAAVSAITV
     TVRDSASPAS SDTATFTLTV TGGATTPAPS TCTGTSVGAG TLTAGRQAAS PSFTRAAGAI
     EVCLDGPSGA DFDVYLQRNY SFFGWITVAQ GTSVNPDEKF AYSASAGTYR VVVKADSGSG
     AYTATVR
//
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