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Database: UniProt
Entry: A0A1S8TXY6_9CLOT
LinkDB: A0A1S8TXY6_9CLOT
Original site: A0A1S8TXY6_9CLOT 
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
//
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