ID A0A1S8TXY6_9CLOT Unreviewed; 573 AA.
AC A0A1S8TXY6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Subtilase family protein {ECO:0000313|EMBL:OOM82550.1};
GN ORFNames=CLPUN_00820 {ECO:0000313|EMBL:OOM82550.1};
OS Clostridium puniceum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=29367 {ECO:0000313|EMBL:OOM82550.1, ECO:0000313|Proteomes:UP000190890};
RN [1] {ECO:0000313|EMBL:OOM82550.1, ECO:0000313|Proteomes:UP000190890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2619 {ECO:0000313|EMBL:OOM82550.1,
RC ECO:0000313|Proteomes:UP000190890};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATPase C chain family.
CC {ECO:0000256|ARBA:ARBA00006704}.
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:OOM82550.1}.
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DR EMBL; LZZM01000006; OOM82550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8TXY6; -.
DR STRING; 29367.CLPUN_00820; -.
DR OrthoDB; 2744137at2; -.
DR Proteomes; UP000190890; 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; IPR020537; ATP_synth_F0_csu_DDCD_BS.
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; IPR023827; Peptidase_S8_Asp-AS.
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; PS00605; ATPASE_C; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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:UP000190890};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 104..305
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 442..561
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 506
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 573 AA; 63508 MW; A0BB26ED2F0D63B1 CRC64;
MRASFRAPQN IFSDPNYYHY IVQYQGNIEE EVSKYSGYYV TIINDKYAII SANRELELNI
EGPMFSTIVY ASPPDVFTLE EISPIEASGA NFLQLELPLR LTGVGVTVAI IDTGIDYLNE
EFIKENGETK IEYIWDQTIN SNEESKSDFG VPFGTFYSKN NIQEAINAYR QGRSPYEIVP
TIDEIGHGTN MAGIIGAIGR NPNLKGIVPE CSFVIVKLIE SIAYKRLFNV KVPIFDIVAI
FTALEFLYRD SLINNKPIVI YFPLGSNLGS HKGNGILEQY IDSISRNSGI AIVTGTGNQG
ASETHTSGSI TQVGENRTIQ LYMSSEQEYN VVDIWIDSPN IMSLAIISPS GESTETISVE
INTLKTYSFV FENTSVKINY YLPEENTGDQ LIRIRFFNIK EGVWRLKLTG QSILDGKFNA
WMLQEGLSIR GTKFISSDPY GTIMNPATSS YIITAAAYNQ NNNTILSYSG MALLDDYIDR
IDVAAGGVNA LTVAPNNQTA IVNGTSVAAA ILVGACAMLF QWGIVEGNYP NIYSQTIKTY
ISRGAVQRSG DSYPNPQWGY GILNILKMFQ NML
//