ID   A0A1M6WLG9_9BACT        Unreviewed;      1245 AA.
AC   A0A1M6WLG9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Subtilase family protein {ECO:0000313|EMBL:SHK94567.1};
GN   ORFNames=SAMN05720469_12530 {ECO:0000313|EMBL:SHK94567.1};
OS   Fibrobacter intestinalis.
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=28122 {ECO:0000313|EMBL:SHK94567.1, ECO:0000313|Proteomes:UP000184275};
RN   [1] {ECO:0000313|Proteomes:UP000184275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWOS {ECO:0000313|Proteomes:UP000184275};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FRAW01000025; SHK94567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6WLG9; -.
DR   Proteomes; UP000184275; Unassembled WGS sequence.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-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   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1245
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012816516"
FT   DOMAIN          421..628
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          820..905
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        430
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        469
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        848
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1245 AA;  141889 MW;  D167D6B755F94C28 CRC64;
     MKRYVLLVFF CSFASAMDSL SVRLVSERHR TEWNWVEYRI SLVNKSNIPI LNPEIRYFAE
     NSWIQFCERN KINSRCKESN GGLYLKDSLL TLSVDYVTWP FSVSPSIFSD GKWSTIKLKM
     KGMFYPGSNV DIYFRIYRND WGAWDCSRDF SYQKNSNFVE ENYQMAVYDA SSQLLWGYDP
     TSGRYSIKDV LWQDRRENFL VQKFDGNSNE VIPAGRFWLL KDVPLLSKER ILLKERGLKP
     LEAGRIQNKN LYLFRSEIPI KKFTLDSLLT NFYNAIVADD TTRLSIDFFR TEFSYEKKDS
     CESIGVCKDD SLSRTEFDLF ISCWPDVTMG DCKNIAIGCG GLRAEIDRNL VVSTHTKETL
     SCLEINQNIR HIDVSRESKP VNDKGRKAIN IDVLQNNEAW KNALLMQQPT TNWLSDADYT
     GEGIVVGVYD SGILYNHSTF NEVAATGELV QRKLAGESKI ECKFNDCEHG SHVAGIIGGN
     GWKSGSAANG RDNFLYRGVA PKVNFYANRM FVLHQKGNVV NHSHINDFSG LYEFNSYTMD
     YNLFYDWKNC EDECDSISKA SIYAAANNGG LTPQYGNLLS YHSILANTKN STVVGNMSSV
     TSVRNSTSSM GPTWDGRIKP DLMAPGSGAE FRFDENAPLV LLIDYFRMYH KNAETPFFEL
     NFGTNDSLLN PDLRRKNCIY LSESPEQLIK CNLFREKFVG KLEYLDDALA SNGKALKWTE
     NRLSAQESYV NWRYELFSAT PFEVQQDDEI EIRFRRISGK IDYPIINGSV YFSSEDDFYD
     GYETTSVRWI LGKIGDDYQT TRFPWNGKSL VSNFLRFGFN YDYGIVSSVP CKQFEDEMSC
     YGESSGTSMA APFVSGIAAL MYQKFRTKTG LSLDKFSMRN STVKAILIHT SIDMEDSQQA
     HVAYNSDISA AEHDGNLYYT PYGKGPDFAT GWGRVDAESA LGYIEDYDET SKSFSRFREF
     DISNGQEKNW SIYVPEGVHS LRATLVWDDA PGMRDDGNVP VVSSLDSKLI NDLDMYFISP
     SGKFYFPWRL RPLPTNKIDF NGNLIQETFG LENIHKSDIQ EAERFCGKND KLSGECFDHL
     NNVEVVDVDF PEKGKWQIVV RGTRIVQGND SSGNAQVASI VSDLRLWNST CQIVHPYLSQ
     NRLVCEYALG DNLESFVTFN KQTYVGKGDS IFLYDDKNHL LGTYTGTGLS GKRIKVRGKK
     LKVILDSDND DSQGYGFEIS RIEKVPYSIL PMLFETSKKR KMINE
//