ID A0A0X3VE80_9ACTN Unreviewed; 497 AA.
AC A0A0X3VE80;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KUL43111.1};
GN ORFNames=ADL22_13625 {ECO:0000313|EMBL:KUL43111.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL43111.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL43111.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL43111.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
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 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:KUL43111.1}.
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DR EMBL; LLZI01000146; KUL43111.1; -; Genomic_DNA.
DR RefSeq; WP_066977832.1; NZ_LLZI01000146.1.
DR AlphaFoldDB; A0A0X3VE80; -.
DR STRING; 1609095.ADL22_13625; -.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000053256; 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 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 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; 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:UP000053256};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..497
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007055913"
FT DOMAIN 171..488
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 430
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 497 AA; 51077 MW; 309651C1026FFB93 CRC64;
MARPLAHPRK RRLRALAVPV GLALTASLGF LPGAAGAAAP ADSGPLLSYV VNTVPDHATV
GAVERAIDRA GGKVITAHER IGVIVAHSAN PRFAATLRTT PGVQSAGATR TAPLKQTGTD
DVGKPQRITA AQLAAAERTA KAKGGEPLEP LQWDLPAIKA DQAAKVNPGS RKVTVAVIDT
GVDDTHPDLK PNFSARQSAN CVGGVPDTSP GAWRPYDPVE DAHGTHVAGT IAAARNGVGV
AGVAPGVKVS AIKVSEPKTS LFYAESVVCA FVFAADHGVQ VTNNSYYVDP WMFNCKDDAD
QAAIVDAVGR AAKYAQDKGV VNVAAAGNAN ADLAADKLTD TGSPNDSTPV TRTLSPKTCW
DVPTQLPGTV TVAATGSHRL KSGYSNYGLN QIDVAAPGGD SKQLPDLPAK NGNILSTIPG
GDWAFYAGTS MASPHVAGVA ALLKSAHPKA GPQEIQWLLK QQADNPGCPA TDRTCTGTPQ
LNSHFGYGIV NALKAVE
//