ID A0A0L6ZEZ1_9CLOT Unreviewed; 1703 AA.
AC A0A0L6ZEZ1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Thermophilic serine proteinase {ECO:0000313|EMBL:KOA21343.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:KOA21343.1};
GN ORFNames=CLHOM_02280 {ECO:0000313|EMBL:KOA21343.1};
OS Clostridium homopropionicum DSM 5847.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121318 {ECO:0000313|EMBL:KOA21343.1, ECO:0000313|Proteomes:UP000037043};
RN [1] {ECO:0000313|Proteomes:UP000037043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5847 {ECO:0000313|Proteomes:UP000037043};
RA Poehlein A., Beck M., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA Duerre P.;
RT "Genome sequence of the strict anaerobe Clostridium homopropionicum LuHBu1
RT (DSM 5847T).";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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:KOA21343.1}.
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DR EMBL; LHUR01000007; KOA21343.1; -; Genomic_DNA.
DR RefSeq; WP_052219838.1; NZ_LHUR01000007.1.
DR STRING; 36844.SAMN04488501_13010; -.
DR PATRIC; fig|1121318.3.peg.226; -.
DR Proteomes; UP000037043; 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; cd00063; FN3; 1.
DR CDD; cd07473; Peptidases_S8_Subtilisin_like; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 4.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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; IPR034204; PfSUB1-like_cat_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50853; FN3; 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:UP000037043};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1703
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005570355"
FT DOMAIN 1220..1314
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 58..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 316
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 700
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1703 AA; 184437 MW; C2CCCB75E566268A CRC64;
MKKRRLTILS LSLSALLLIP QNVMAITQSV ITTQPSTSST VKSVAYVENN GKLQYLKQGS
SSASSSSNTS VSASSSTTAS GSKVTKARKS QLKGTANNSG SIQKPTSTNP KETAQDKIKN
AKNKLRPTSV SNQLIIKFKN GTTDTVKNSI YSKNNLKSKK NIKALNTSLV ELPKGTTVEQ
ATKFLKANSN VESVQPNYLY YPSDATISSD PRSSELWGLE NVGQAINGVS GAPDIDINAP
TAWNVTKGDS NLVVGIIDTG VDYKHPDLID KVWTNPGETP MNGVDDDNNG YIDDVHGWDF
YNNDNSVFDI NDGDFHGTHV AGTIAASMND VGVVGVAPNV QIMPLKFIGP DGGDTMAAIE
AINYAANMGI KITNNSWGGG GYDPLLKEAI ENSNSLFVAA AGNESNNNDM YNSYPASYDS
NNILSVAAVE NDGTLAGFSN YGPATVDVAA PGVSILSTVP KNYDLGAAIG SSNGTYKTLY
QGFGLESIAI PPLAEDYMSK VLNYFGITSG DKILLVQDDE HDAPAVFPNY FAAYKNPLDV
LVPTVGFTVD TQTVGYNSAG PDAAVLNQYK LVIWFTGDGF GWSSMPFEGA LRAADRTNLS
NYLNQGGNLF LASKEAAFDT NSLPFINTYL HANLAYEDEG EGRPTVAGLP NTAFAGSLYP
LMPSLYIDYL EPSDPIGQIV LNYPGDPDYS NAYDYYNGTS MATPHVTGVA ALLLSKNLTQ
NPLELKSKIM KSSQFLPSLI GYVGTCGLVR ADAALALADF QADDDIPGLP LPQSPVVGTL
DETSDLDDVY SFNLDMGEMI TFTLTGDPNT DFDLHIYDGM ATTVNTAYGL LASSENIGST
ESITFTATHP GVYYIDAYAY SGAGDYTLSY EKAGNIVFDD KDPLLAFIGK WTDDLSENHY
KGSAKTLNSS GTMILPFTGS KVTWKGFKGP NQGIANVLID GQNRGAVSLY SITKEFNQEL
FTADLPYGHH TLEIQWTGRW DKAAKRKTYT AINVDSIEVA NINKPMAPQS LTTERFLNAV
NIVFFIQDYN AIKFNVYRSE NGVDFTKIDS RPVSAPDAHY LDRDLQDKLY YYKITTENPL
GIESDFSDVV QDRPIVGNSK FTIDDSSNHI TYTGAWTEEN KIGAYKDKVH STTQAGAKAS
LPFTGYNLGF KFYGGPGMGT VRITSSFGFF WDLDLSQYPD ATSIRLYSTP RVEGDTWTIE
CLSGKVMFDG MDIEDLQTTP PAAPSTLKAA KDDSNVNLTW NDNSEIDVAG YNVYRSETKG
AKGTQINTAL VGDLKFTDSS VDATKTYYYT ISAVNYAKLE SGASNEVEIL GQAGGGTTVT
RVEETDANVK FSTGWTLDSN ANNSGASAKY SNVTGSYVEF TFTGTGIKWL YLANQYRGIA
KVTIDGVSEN VDTYSSTTQY KKVAYTKDNL TYGQHTIKIE VTSTKNPSAL GTHLHVDAFE
VITTPQPTIT RFEETDTNVK FSSGWTLDSN ANNSGASAKY SNVTSSYVEF TFTGTGIKWL
YLANQYRGLA KVTIDGVSEN IDTYSSTTQY KKVAYTKDNL TYGQHTIKIE VTGTKNPSAL
GTHLHVDAFE VITAPQPTIT RFEETDTNVK FSTGWTLDSN ANNSGASAKY SNVTGSYVEF
TFTGTGIKWL YLANQYRGIA KVTIDGVSEN IDTYSSTTQY KKVAYTKDNL TYGQHTIKIE
VTGTKNPSAL GTHLHVDAFE VIQ
//
