ID A0A0A3J901_9BACL Unreviewed; 306 AA. AC A0A0A3J901; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 29-MAY-2024, entry version 27. 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. 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:KGR83517.1}. 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; JPVQ01000087; KGR83517.1; -; Genomic_DNA. DR RefSeq; WP_036180552.1; NZ_JPVQ01000087.1. DR AlphaFoldDB; A0A0A3J901; -. DR eggNOG; COG1404; Bacteria. DR OrthoDB; 9798386at2; -. DR Proteomes; UP000030595; Unassembled WGS sequence. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. 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; 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; 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 //