ID A0A1I1S7K5_9CLOT Unreviewed; 1779 AA.
AC A0A1I1S7K5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Subtilase family protein {ECO:0000313|EMBL:SFD40578.1};
GN ORFNames=SAMN05421842_14211 {ECO:0000313|EMBL:SFD40578.1};
OS Clostridium uliginosum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=119641 {ECO:0000313|EMBL:SFD40578.1, ECO:0000313|Proteomes:UP000199263};
RN [1] {ECO:0000313|EMBL:SFD40578.1, ECO:0000313|Proteomes:UP000199263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12992 {ECO:0000313|EMBL:SFD40578.1,
RC ECO:0000313|Proteomes:UP000199263};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; FOMG01000042; SFD40578.1; -; Genomic_DNA.
DR STRING; 119641.SAMN05421842_14211; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000199263; 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; 3.
DR Gene3D; 2.60.120.1290; -; 3.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 3.
DR InterPro; IPR034045; Pep_S8_CspA-like.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 6.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 3.
DR PROSITE; PS51892; SUBTILASE; 3.
DR PROSITE; PS00136; SUBTILASE_ASP; 3.
DR PROSITE; PS00137; SUBTILASE_HIS; 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:UP000199263};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 117..239
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 450..575
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 696..888
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1028..1139
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1270..1387
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1610..1728
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 520
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 703
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 772
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1094
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1279
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1351
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1673
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1779 AA; 195373 MW; AC23076A0E8FFEAE CRC64;
MVEGGISIKK SKILKKNYRQ TSNDVFTGEN AAYALVEYSG DISKAVSKIT NTKVFIIDEN
TALLSVIDAD IDDIVSKLSD VITYRNPGSI YTLCAISPVE ASGAEQFHNN EYLPLDGSGV
IVGIIDTGID YLNEEFINTD GTSRILTILD QTINTGKRPS NQPIGSEYSA EDINNAIKAN
KEGKNPYDIV PSKDEIGHGT NMAGIAAARG ARPALLGAAP KCDLAIVKLV PASKKLKEES
YVYGDAPIYS SIAVFSGIKY LYELSMNLKK PIVILIPLGY SMGAHNGLAF NERYIDEVSR
IRGVAVVVPT GNEGDADTHT SGVIAKNGDL ANIELIVDKK QKNLRFEIWI SKPDKLTLSI
TSPSGEIVDR IAPVNKKVTE INFIYEKTKM FIQYLKPEEI SGDEKINITA INIAEGIWNF
KLVGEMVSVG KYDAYLPQKA IIAPNTKFLS PNPDGTLMIP STSRYAISVG YYNQTNNAIE
VDSGRGYTRD NRIKPDIVAG GVNSLMTYGK DGDKIISGSS VAAAVVTGCC ALIFQWGIVQ
GRDRSMYSIK LKTYLIRGTS KREGDEYPNP LWGYGSINMK GVFDNIRGLK KQDNRAVEEH
PNYFFDIRNK IFLIEYKADI VNSLKRFPNT EVFIIDEKRA IITTPYEIYD DVVKLTPEIV
YVDLDDAYTT CDISPVEASG ATVFHNNVYL PLNGFGVIVG IIDTGIDYLN EEFINEDGTT
RILTIMDRSI PDNTSKFKCA VYKQEDINKA IETKKSGGDP YKIVPSKDEI GHGTNMAGII
AARGATPGLI GAAPRCNLAI VKLNPASKAF RNYYQIYGNE PVYQNPGILL GIKYLYDLSV
ELKKPIVIYI PLGANTGPHN GQAFIEKYIT EISNYNGVAV VAPTGNQGNT DTHTSGIIKN
KGDESIVEIQ IGKNQQDIRI EIWISKPDKV ALSITSPTGE AIRKISPKLK SMTDITFLYE
ETKMTIEYFI PEELTGEQKI VIIASNIREG IWQFKLIGEL IVVGKYDIWL LQRELLAPDT
KFLNPISTTT LTTPGTSKGA ITIGYYNQNN NSIIPESGKG YTRDNMIKPD IAAGGINTIT
TSVGGGTQII SGSSVAGAVT AGACALLFQW GIVDGNDSPM FAIKLKTYLI RGASKRQRDV
YPNPQWGYGM LDIKGVFDNI RGLKIEENRE TQLNKKINYF LEPNNINTIV EYNGDIVSAI
KKFQNSDVYI IDEKRAFIAL PYEINSKVLK TTKEIIFADP GSALTLCDIS PVIASEATLF
HNSEYLSLDG SGVIVGIVDT GIDYLNDEFI NNDGSSRIIS IYDQNVESDT IQPEIIAGTV
YTQDNINKAI QAKKNGGDPY AIVPSKDEIG HGTKIAGIIT ARGANPELIG VAPKCSLAVV
KLRTGNKVFR QVYALYGNEI SYKNTSVFLG MKYLFDLASK LNKPIIIYIP LGTNMGAHTG
ESLVERYSDE ICKNIGVAVV APTGNQGNTA THTSGTIKSS GDIGIIELKI GEKQKDIRIE
IWVSKPDKVA LSITSPTGEV IKRIPPKLKE IIDITFVYEE TKMTIEYFIP EEISGDQKIV
IMARDIREGI WQFKLIGELI IVGRYDAWIL QRELIAPDTR FLRPNPYITL TLPGTSSSVI
TAAYYNQNNN SIVPESGRGF TKNDVIKPDI AAGGVNAKTT SVGGTTAIIS GSSVAGAVVA
GACALLFQWG IIDGNDTTMY AEKLKTYLIR GAQERPGDVY PNPQWGYGRL SLKGIFDNIR
LAKDNKVINY NREREKPRNE YYVGNLFIRL PENYNTDYL
//
