ID A0A1I5ITT9_9FIRM Unreviewed; 387 AA.
AC A0A1I5ITT9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Serine protease AprX {ECO:0000313|EMBL:SFO63974.1};
GN ORFNames=SAMN04489757_1537 {ECO:0000313|EMBL:SFO63974.1};
OS Anaerocolumna aminovalerica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerocolumna.
OX NCBI_TaxID=1527 {ECO:0000313|EMBL:SFO63974.1, ECO:0000313|Proteomes:UP000198806};
RN [1] {ECO:0000313|EMBL:SFO63974.1, ECO:0000313|Proteomes:UP000198806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1283 {ECO:0000313|EMBL:SFO63974.1,
RC ECO:0000313|Proteomes:UP000198806};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ECO:0000256|RuleBase:RU003355}.
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DR EMBL; FOWD01000053; SFO63974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5ITT9; -.
DR STRING; 1527.SAMN04489757_1537; -.
DR Proteomes; UP000198806; 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; cd07487; Peptidases_S8_1; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 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; IPR037045; S8pro/Inhibitor_I9_sf.
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:UP000198806};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 89..378
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 98
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 332
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 387 AA; 42624 MW; 5BE498259F536D57 CRC64;
MKKKEKVQII VQCSEYENNY EQVKSMGKIK YKLPMIDSYV IEVNEERLDY LQSKHELLSF
ELDTHITAQM NRASEIIELK WAHERNIMGE GIGVAVVDTG LCLHKDFTEG TNRVKGFYDL
IHGRTEPYDD NGHGSHVAGI IGGSGFLSNG KYVGVAPKCD LLGIKVLDQK GDGNISDVLA
GLQWIIDNRE KYNIRIVNIS VGTTTKDNID ENSLLVKGVN AVWDSGIVVV VAAGNNGPGP
MSISTPGISR KVITVGSSDD RISVELFGSK TMDYSGRGPT AACIKKPDII APGSNIISCG
TMKNYQRYRY NLKNNPRSDA YNIMYTVKSG TSMATPIVSG AIALLLSRYP YMTNKDIKLK
LRESAIDLGQ PWAKQGWGLL NIPRLLS
//
