ID A0A0U4BLH4_9BACT Unreviewed; 514 AA.
AC A0A0U4BLH4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:ALW87419.1};
GN ORFNames=AUC43_16740 {ECO:0000313|EMBL:ALW87419.1};
OS Hymenobacter sedentarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW87419.1, ECO:0000313|Proteomes:UP000059542};
RN [1] {ECO:0000313|EMBL:ALW87419.1, ECO:0000313|Proteomes:UP000059542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5B {ECO:0000313|EMBL:ALW87419.1,
RC ECO:0000313|Proteomes:UP000059542};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP013909; ALW87419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4BLH4; -.
DR KEGG; hyg:AUC43_16740; -.
DR Proteomes; UP000059542; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07483; Peptidases_S8_Subtilisin_Novo-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
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; IPR034080; Protease_P7-like_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 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:UP000059542};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 40..485
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 46
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 439
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 514 AA; 55647 MW; EA2201A1A32B62DE CRC64;
MGDLSSSQWY LKDPTLDKVP GVGATRVYDE ILKTLTPQPV VVAVIDSGID TAHVDLKPML
WTNPKEIPNN GIDDDKNGYV DDVHGWNFLG GADGRNVNAE TLEMTRIVAA GRKRFKGKTA
ATVKPTERAD FALYTKAEKA YSARLKEETE RSEQVESMTG PLTMMVDNLK QALGVTTLDT
TALRTIKTDD PNLRRATAGM LEMMRQTGAA DTDALLKELS EGAKQERSML DNSLNLKFNP
RADIVKDNPN DVTERYYGNN DLHGPDPMHG THVSGIIAAV RDNQLGVQGI APNPVRIMVV
RAVPDGDERD KDVANAIRYA VDNGAQIINM SFGKEFSPQR QAVEAAFKYA ASKNVLLVHA
AGNENANLDV TSNYPASFYI NKTTVPNLLT VGASGPRDNA QLPANFSNYS KRAVDVFAPG
MSIFSTLPGS KFGNESGTSM ASPVTAGVAA VLKSYFPKLT AADLKRIIMQ SARVHHTKVQ
VPGTDKMVDF STLSVTGGVV DLYEAVRLAQ KASL
//
