ID A0A1Y3QWG9_9FIRM Unreviewed; 633 AA.
AC A0A1Y3QWG9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=BAA04_07965 {ECO:0000313|EMBL:OUN00910.1};
OS Firmicutes bacterium ZCTH02-B6.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1861639 {ECO:0000313|EMBL:OUN00910.1, ECO:0000313|Proteomes:UP000196077};
RN [1] {ECO:0000313|Proteomes:UP000196077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nascimento L., Pereira R.V., Martins L.F., Quaggio R.B., Silva A.M.,
RA Setubal J.C.;
RL Submitted (JUN-2016) 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:OUN00910.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LZRQ01000047; OUN00910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3QWG9; -.
DR Proteomes; UP000196077; 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; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
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; EXTRACELLULAR PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 261..521
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 308
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 474
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 633 AA; 66170 MW; E0A45FEFCD6EF31F CRC64;
MIRAAGREAT TGQDGTFALE DLPVQGQTMT VTVTAPGYEP ATVAIHPSGG ANLLVTIVLV
PNEDDGGSSG NDGEQGEDGG TGPGGDDGDG GDGGNRDDES PEPRPEPEPV YRGAVEANVR
LVNVGNPQVA AAAVVPQELL SRHAARTVTR TTAEAVPGEW IVQLNGEYPV QAINTMWTDA
GVRVVERLAD NFYLVAADGA GSSVETELRL AQLPNVVSIE PNKRVQPVAV SYLPNDTYFD
RQWSLPLVSI PYAWNITTGS RDVVVAVLDT GILPNHPDLQ GVNIISGRNF ASDQSATNYT
DDATSLSHGT MVAGIIGAMT NNGQGIAGIN WSVSIMPVRV MSSRSGGTVA AVGQGIRWAA
DNGAHVINMS LAWDATYNDT FVNQQIEYAA SKGVVLVAGA GNDSGRVTMP AAHPDVIAVG
AVDRNKRVAW YSNYGSQLEL VAPGGDTRSS QANGILSTDI VSRRLSYSYQ QGTSFASPHV
AGIVALMYSA GITDANEIRE LLRHTAEDLG APGFDNYYGY GLVNAYAAVT GSDPIKAQVA
VASADGTRIW GPVTPLRSGA RALARLEGVA PGEHTLFAWI DAVPDGMLGD GDFAGVTQVE
VPEDGTVTAD LVLAVWETLS AQDRARLSAL ANR
//