ID F2JJD4_CELLD Unreviewed; 329 AA.
AC F2JJD4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Subtilisin {ECO:0000313|EMBL:ADZ85529.1};
DE EC=3.4.21.62 {ECO:0000313|EMBL:ADZ85529.1};
GN OrderedLocusNames=Clole_3849 {ECO:0000313|EMBL:ADZ85529.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ85529.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ85529.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP002582; ADZ85529.1; -; Genomic_DNA.
DR RefSeq; WP_013658803.1; NC_015275.1.
DR AlphaFoldDB; F2JJD4; -.
DR STRING; 642492.Clole_3849; -.
DR MEROPS; S08.030; -.
DR KEGG; cle:Clole_3849; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_0_9; -.
DR Proteomes; UP000008467; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR034202; Subtilisin_Carlsberg-like.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 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:UP000008467};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 42..293
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 51
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 88
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 329 AA; 35868 MW; 8CBB70FBFD3C73E4 CRC64;
MSDSTMKLAN YQLIEVQKEV YKLPKGVDLI GASKLWEQGE KGRGVTIAVI DTGCDTEHIE
LKDRIIGGRN FTEEDEGNAN IYKDYNGHGT HVCGTIAASM NGTGVVGVAP EASLIILKAS
NKKGIARYSS IINAIYYSIK IKVDIISLSL GGEADNEMLH EAIREAIRHN ILVVCAAANE
NADGLPMISY PADYDECISV GSVDYGNLNK QMKRERHLDL VAPGVGILST YLDGTYAKMS
GTSMAVPHVT GALALLMNYC KKEFGRKLTE SEMYAQLIKR TINFGYTPAE VGNGCIFLTA
IDLVRDCYNQ TLNDIEKCKK DSSKSDKST
//