ID   A0A0A3J901_9BACL        Unreviewed;       306 AA.
AC   A0A0A3J901;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   03-MAY-2023, entry version 24.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=CD30_19405 {ECO:0000313|EMBL:KGR83517.1};
OS   Ureibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Ureibacillus.
OX   NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR83517.1, ECO:0000313|Proteomes:UP000030595};
RN   [1] {ECO:0000313|EMBL:KGR83517.1, ECO:0000313|Proteomes:UP000030595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR83517.1,
RC   ECO:0000313|Proteomes:UP000030595};
RA   Zhang F., Wang G., Zhang L.;
RT   "Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       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:KGR83517.1}.
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DR   EMBL; JPVQ01000087; KGR83517.1; -; Genomic_DNA.
DR   RefSeq; WP_036180552.1; NZ_JPVQ01000087.1.
DR   AlphaFoldDB; A0A0A3J901; -.
DR   STRING; 1211035.CD30_19405; -.
DR   EnsemblBacteria; KGR83517; KGR83517; CD30_19405.
DR   eggNOG; COG1404; Bacteria.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000030595; 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; IPR022398; Peptidase_S8_His-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; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030595};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        5..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          50..276
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        58
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        85
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        241
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   306 AA;  33948 MW;  E7B5E32C5F43DFB9 CRC64;
     MRRGIIISPL IIYFILFFVL FKHDSDETFN TELNKFINIE QIDYSIFLMK DIKVGIIDIG
     FINDHPNLNI VPINDVEMKD EHNIHGTVVA GIISSQKSNV NNFSGIIPGI TVYTYSLPYE
     NDISVSALTE GLKVMNEYQM DVINISLATG EESIALKNEI KKAVSQGTVI VASAGNYPNN
     LNYYPAAYKI PGVISVGAID REFNLLENTT YNNYIDVWTL GEDVLSLSIN PESVKYYSGT
     SVATPIVTSL VAMLKAKCGK ISSSPREIEN MLLKGATPII QSWNGFNVNT RIVDFKNTLL
     NCEGLL
//