ID A0A176U1Q4_9FIRM Unreviewed; 589 AA.
AC A0A176U1Q4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase, S8/S53 family {ECO:0000313|EMBL:OAD86422.1};
DE Flags: Fragment;
GN ORFNames=HMPREF2738_03618 {ECO:0000313|EMBL:OAD86422.1};
OS Clostridiales bacterium KLE1615.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1715004 {ECO:0000313|EMBL:OAD86422.1, ECO:0000313|Proteomes:UP000077212};
RN [1] {ECO:0000313|EMBL:OAD86422.1, ECO:0000313|Proteomes:UP000077212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1615 {ECO:0000313|EMBL:OAD86422.1,
RC ECO:0000313|Proteomes:UP000077212};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:OAD86422.1}.
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DR EMBL; LXPQ01000261; OAD86422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176U1Q4; -.
DR PATRIC; fig|1715004.3.peg.3618; -.
DR Proteomes; UP000077212; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07478; Peptidases_S8_CspA-like; 1.
DR Gene3D; 2.60.120.1290; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034045; Pep_S8_CspA-like.
DR InterPro; IPR017310; Pept_S8A_subtilisin_clostridia.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PIRSF; PIRSF037894; Subtilisin_rel_CspABC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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:UP000077212};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 96..318
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 448..573
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 105
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 519
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OAD86422.1"
SQ SEQUENCE 589 AA; 64779 MW; CA2FDE5B28A3D3B2 CRC64;
VLGSLFLNCQ DQIYSEEYSD FIGNRSLIES KYALDCKQPL GAMFASLYLK LSDGYEDGTV
YGYYNIPKLF GLQDTGSMEA SGILQVRENP DLKLDGSGVL IGFVDTGIDY AGSIFLKQDG
TTRVIAIWDQ TIPAESPIRL PELPTTLENI TRTPEGFLYG SEFTHEQLNA AVKMEDTYEG
ISSRDENGHG TFLASIAAGN ELPDGSFTGA APKADIAMVK LKPAKNRLRA YYQIKEDAVA
YQENDIMAGV LYLVSLAKKR QQPLVICLGL GTNAGSHRGG LPLARMLEEL GSSVGITIVA
GTGNETARGH HFEGQISSES GYEDVEIRVA EGENGFFLEL WANAPETYSV AIRSPNGEVI
PRIYVRPGRI EVLNFALAQT RVEVSYRLSV TGTGEFLALL RFINITPGVW TVRVYNDLFI
TGHYHMWLPI ESFLRQDTVF LRPSEFITLT SPSDAANVIS VSNYNHQNNS IYLYSGRGYT
TDGRICPDLA APGVGIEGFT SSLSGVGNEL RRVQRSGSSA AAAHMAGAAA LFCQWTRESG
IRYFSSTDVR TYFIRGAKRD SSRTYPNREW GFGTLDLYGV FRNLQTQIF
//
