ID A0A0F7JT86_9DEIO Unreviewed; 454 AA.
AC A0A0F7JT86;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=SY84_13985 {ECO:0000313|EMBL:AKH17943.1};
OS Deinococcus soli (ex Cha et al. 2016).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH17943.1, ECO:0000313|Proteomes:UP000034024};
RN [1] {ECO:0000313|EMBL:AKH17943.1, ECO:0000313|Proteomes:UP000034024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N5 {ECO:0000313|EMBL:AKH17943.1,
RC ECO:0000313|Proteomes:UP000034024};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus soli/N5/whole genome sequencing.";
RL Submitted (JAN-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}.
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DR EMBL; CP011389; AKH17943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7JT86; -.
DR KEGG; dch:SY84_13985; -.
DR PATRIC; fig|1309411.5.peg.2847; -.
DR OrthoDB; 5240330at2; -.
DR Proteomes; UP000034024; Chromosome.
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; IPR023828; Peptidase_S8_Ser-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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000034024};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..454
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002517276"
FT DOMAIN 191..433
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 400
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 454 AA; 44523 MW; 91C0982909C1E4D1 CRC64;
MRLPVPVLCA VTLSLLLSAC GGGGGGTITP VPEPTPAPAP TPGPVCTQSL SAQPAPAAAP
VGGTAWMAGA ADWSRPHVPG RVLVSSAVSG PALSTLGVTG QEVVPGVTVV TTLPGAEASV
AGRLQAQGAV IQPDYLYVPL AVPNDPGVPG NGGVTVGGAR YEQTYLTRVN APQAWTFLQS
CGKTPVAART AVLDSLVNEA HPDLQGRLSA GRSYLAGGPS DDGGHGTATT GLIAATTNNG
QGLAGLTWTG SVTPMEVIGA SGASTSTVAQ AVRDAVSGGA LVINMSLGIA VTGTTDPDPV
LSKALTDAAK SAVLVASAGN TAGDGLYYPA SHPEVIAVGA AGSGDTLACY SARPLAGQTA
QAAQFMIAPG GAGNCPGATN ATQLLVLNQG SGYTLQAGTS FAAPLVSGAA ALMRAANPAL
SSQETKSRLL ASTRLTAEGV RFLDVNAAVR SATR
//
