ID A0A101J871_9ACTN Unreviewed; 478 AA.
AC A0A101J871;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KUL21965.1};
GN ORFNames=ADL12_43470 {ECO:0000313|EMBL:KUL21965.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL21965.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-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 -!- 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:KUL21965.1}.
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DR EMBL; LLZG01000401; KUL21965.1; -; Genomic_DNA.
DR RefSeq; WP_062713891.1; NZ_LLZG01000401.1.
DR AlphaFoldDB; A0A101J871; -.
DR OrthoDB; 5177045at2; -.
DR Proteomes; UP000053923; 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; cd00306; Peptidases_S8_S53; 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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF7; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-1 PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:UP000053923};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 163..442
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 71..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 414
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 478 AA; 51387 MW; C18AC6EBDA385115 CRC64;
MAPQRFHEQF EQIQRTMPDV PLAMGPDDSG EFIYEKGYIL VRDGEDARVV EETVRAHFTA
EPDLVQDHVR RASPQSNRSG ITRIQVGDPG EGDRSGDRTV AHALRALRET EGRAGRRLVS
RNHLVAIAGG VNSCPGDEPV PALLKRGINP AAAEGVHDPD TAVGVLVIDT GLMNDYRSFP
LLAHTEGDAQ VKECDDDGIL QEYVGHGTFI AGLVAAVAPN TDITVRNSLN DAGALLESEF
GEKLFEAVDA GGWPDILSLS AGTSNGRTDA LLGVEAFMQE LRGRRTLLVA AAGNNGSATP
FWPAAYADVP DYQDVVLSVG ALREDGEFGA CFSNHGGWVK VYAPGERLTS ALTGFDEPVP
YVYQHSTYDA CRYGFGYSCT CQSPRHTGVL SEQGRSVKPD QVMFEGLAHW SGTSFATPLV
AGMIAAHMTA QQERDPRVAR YKMLAANSGF AEVRGAHVPA LRPSTWRPAP VVPPAPRS
//
