ID W7D859_9LIST Unreviewed; 361 AA.
AC W7D859;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:EUJ45297.1};
GN ORFNames=PRIP_05533 {ECO:0000313|EMBL:EUJ45297.1};
OS Listeria riparia FSL S10-1204.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265816 {ECO:0000313|EMBL:EUJ45297.1, ECO:0000313|Proteomes:UP000019248};
RN [1] {ECO:0000313|EMBL:EUJ45297.1, ECO:0000313|Proteomes:UP000019248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1204 {ECO:0000313|EMBL:EUJ45297.1,
RC ECO:0000313|Proteomes:UP000019248};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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:EUJ45297.1}.
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DR EMBL; AODL01000007; EUJ45297.1; -; Genomic_DNA.
DR RefSeq; WP_052008731.1; NZ_AODL01000007.1.
DR AlphaFoldDB; W7D859; -.
DR PATRIC; fig|1265816.5.peg.1090; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000019248; 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; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-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.
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};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..361
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039242020"
FT TRANSMEM 298..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..272
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 252
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 361 AA; 39208 MW; 94D565FEBC6C6F5C CRC64;
MIKKLLLIAL AGILFAGSFA FQPVHASKIV ESNREVNQLD EAGSLAKYHD NNINGKNIKI
AILDTGIDTT NRDLIFKKAI NFTSANSADF NDRNGHGTKI AGIIGARKNG EGLIGIAPNS
ELYIAKVAND SGKVAFAEVI KGLNWAVQQK VDIINISLEF GKGNEALKEA IDNAVEHDII
VVASAGNIRA EGDTFKAYPG AYSDVISVGM LNVQGQIYAD EFKEKKVDVY APGEDLTSTY
FDNKMTLDTG VSYATAYASG YAALVMEDKL SHGESISRES LLKTMKADLN QGIDGTPWYV
YTGLVLNIVT VCALLGLVIY SLVYRRKTLP KKWPTKTIWI VIASLVFINV IGRVMVYILS
S
//