ID A0A2Z4UYX8_9ACTN Unreviewed; 570 AA.
AC A0A2Z4UYX8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Peptidase S8/S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:AWZ13632.1};
GN ORFNames=DRB96_16465 {ECO:0000313|EMBL:AWZ13632.1};
OS Streptomyces sp. ICC1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2099583 {ECO:0000313|EMBL:AWZ13632.1, ECO:0000313|Proteomes:UP000250268};
RN [1] {ECO:0000313|EMBL:AWZ13632.1, ECO:0000313|Proteomes:UP000250268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC1 {ECO:0000313|EMBL:AWZ13632.1,
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; AWZ13632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4UYX8; -.
DR Proteomes; UP000250268; Chromosome.
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 CDD; cd00146; PKD; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; 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; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
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; PF00082; Peptidase_S8; 1.
DR Pfam; PF18911; PKD_4; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF49299; PKD domain; 2.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50093; PKD; 2.
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}.
FT DOMAIN 396..477
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 509..570
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 570 AA; 57685 MW; 9F6840C7551A9C14 CRC64;
MSGTLALPAA VAFSAPASSS PTAEILGADR PGAIAGSYIV TLKDTATLRS RGVPGATGDL
AKRYGGEVGH VYTTALNGFS VKLGEAAAKR LAADPAVARV EADGRAHIAG SQSPADWGLD
RTDQRALPLN NAYTYTQTGA GVHAYILDTG MRNNHGQFDG RWSVGVDTVP GSGQNGLDCN
GHGTHVAGTV GGSTWGMAKA VTLHAVRVLN CDGGADWSWV IAGVDWVTAN AIKPAVANMS
LGGEANATLD AAVAKSINSG VSYAIAAGNS NVDACTVSPA RVAGANTVGA TDITDARASF
SNFGTCTDIF APGVNIESDT WFTAPASQKL SGTSMASPHV AGAIALYLQA NPSASPAQVT
SAMVNAATAG AVTNPGAGSP NRLLYSQGWA APGGPPPPTA SFTNSCNNTT FACSFDGSAS
SDSNGTITRW SWDFGDGTTG TGKTISHTYS KGAVYSVTLT VTDNSGDTGT AGKSFRVGPN
KAPTASFTDG CITYTTIPQM NCFLYGSGSA DSDGTITKWS WTFGDGATST STTNSSAYHS
YVDHGPYTIT LTVTDNEGAT ASVTRSVSKP
//
