ID A0A223D685_9BACL Unreviewed; 381 AA.
AC A0A223D685;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=CIG75_04335 {ECO:0000313|EMBL:ASS77112.1};
OS Tumebacillus algifaecis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS77112.1, ECO:0000313|Proteomes:UP000214688};
RN [1] {ECO:0000313|EMBL:ASS77112.1, ECO:0000313|Proteomes:UP000214688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=THMBR28 {ECO:0000313|EMBL:ASS77112.1,
RC ECO:0000313|Proteomes:UP000214688};
RX PubMed=25858243; DOI=10.1099/ijs.0.000240;
RA Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.;
RT "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum.";
RL Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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; CP022657; ASS77112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223D685; -.
DR KEGG; tab:CIG75_04335; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000214688; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 1.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034084; Thermitase-like_dom.
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.
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:UP000214688};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 129..358
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 381 AA; 38712 MW; EBDD63C39D6786D1 CRC64;
MTASLLPVAG VSAASADVKP AVVANTTGTD QLIVTFKAGK TDVSASVAKA HGASVKKTTA
TGKKILKVDA DKAADVLAQL KADPNVESAE FDQILSVDVT TPNDPSYGSQ YHLTRIQANS
AWDFYTGSTA VKIAIVDTGV DLTHPDLSSK IVAGYNFVSG TTNANDDHGH GTHCAGIAAA
NTNNSTNGAG VDWNARIMPV KVLNAAGSGY TSDISAGVRW AADNGAKVIS MSLGGGSYSA
SFQADIDYAW GKGAVIVAAA GNNGNTAVQY PANYNNVVSV AATTSTDGKA SFSTYGTWVD
IAAPGNAILS TARGGGMTTM SGTSMATPVV AGVAGLVWQR YGTSASPATI VNKIHSTADV
ITGTGSWWIH GRVNAYKAVT L
//