ID A0A0M9ZE93_9ACTN Unreviewed; 400 AA.
AC A0A0M9ZE93;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=ADL00_42335 {ECO:0000313|EMBL:KOV51213.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV51213.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV51213.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV51213.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-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:KOV51213.1}.
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DR EMBL; LGDU01000403; KOV51213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9ZE93; -.
DR PATRIC; fig|1519489.3.peg.9524; -.
DR Proteomes; UP000037758; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000037758};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..400
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005842541"
FT TRANSMEM 369..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..320
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 99
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 287
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 400 AA; 40130 MW; 9A8E657C85707C3A CRC64;
MGRSCARRAC SGGTAAGLVS AAAALSLLLP LPAFAAGRDT ARAEPVELPV MPAVLEAGDP
CTGSSSRMVR AEPAYQRTLN LEQAWRFSRG GGVEVAVVDT GVATGTARLA GRVTPVSGTD
DCVGHGSFLA GIVAAAPATA TRFSGVAPEA RILAVRGTDQ RGTATASTLA AGIRAAADAG
AQVILVGPAL ARKSSELTGA VEHAAARDAL VVAAASPPLR RGEEPGTARD YWPAAQRAVL
SVVGTAQDGS LPDGTAVPKD ADLSAPGSGV IGVGPRGNGY FIGSGSSLAA AFVAGAAALV
RDRYPELSAD ATAERLTRTA YPADVPRMDV YAALSSAAAG REPVAEPPLV PARIPSDEPT
ENAVRRGTLL AGAGAVTAGA VAWAGLVVRL RRRRRHGTTD
//
