ID   A0A2Z4V358_9ACTN        Unreviewed;       587 AA.
AC   A0A2Z4V358;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Peptidase S8 {ECO:0000313|EMBL:AWZ15713.1};
GN   ORFNames=DRB96_29545 {ECO:0000313|EMBL:AWZ15713.1};
OS   Streptomyces sp. ICC1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2099583 {ECO:0000313|EMBL:AWZ15713.1, ECO:0000313|Proteomes:UP000250268};
RN   [1] {ECO:0000313|EMBL:AWZ15713.1, ECO:0000313|Proteomes:UP000250268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC1 {ECO:0000313|EMBL:AWZ15713.1,
RC   ECO:0000313|Proteomes:UP000250268};
RA   Gosse J.;
RT   "Whole genome sequencing and metabolomic study of cave Streptomyces
RT   isolates ICC1 and ICC4.";
RL   Submitted (JUN-2018) 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}.
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DR   EMBL; CP030287; AWZ15713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4V358; -.
DR   Proteomes; UP000250268; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; 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   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000250268};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..587
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038705581"
FT   DOMAIN          471..587
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        403
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   587 AA;  59360 MW;  9FA44CB9DBCED09B CRC64;
     MLAAALGALA FGAPAALAGT APVSPVGTPA ASAPAKAQAA APTSQSATWA AGTRAYLVIT
     AAGDSSAVRS AVTANGGTVF SYFDSIGVIV AHSTSSTFAT TMRGVSGVQK VGATRTSDVP
     ADAYNPALPA NPAQSSTAAG EPVRVDMSQI KADQAWAVNP GSATVKVGIL DTGVDDQHQD
     LAPNFNAADS ASCAYGKADT RVGAWRDVGS HGTHVAGTVA AAKNGKGVVG VAPGVKISSV
     RVAEPSTSMF FAENTICAFV WSGDHGFKVT NNSYYTDPWQ FNCPDNIDQA AIIEGVKRAQ
     EYAESKGSLQ VAAAGNEDYD LAHKTTDSAS PNDSTPTNRT ITNACLDIPT ELPGVVTVAA
     NGTGVTKASF SNFGQGVIDV AAPGSNVYST VPGGTYSSMS GTSMASPHVA GVAALIASAN
     PGITPAQIRD KLATQANDVA CPSDGRCTGT TANNGFFGEG QVDALKAVGA TPPPGKYFEN
     LTDVAIPDNT TVESPVTVSG VTGNAPATLK VGVDIKHTYT GDIKVDLVAP DGTVYTLSNR
     AGGSTDNIIK SFTVNASSEV ANGVWKLRVN DNASQDTGKI DAWNLTF
//