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Database: UniProt
Entry: D9SRH6_CLOC7
LinkDB: D9SRH6_CLOC7
Original site: D9SRH6_CLOC7 
ID   D9SRH6_CLOC7            Unreviewed;      1198 AA.
AC   D9SRH6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADL52405.1};
GN   OrderedLocusNames=Clocel_2705 {ECO:0000313|EMBL:ADL52405.1};
OS   Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL52405.1, ECO:0000313|Proteomes:UP000002730};
RN   [1] {ECO:0000313|EMBL:ADL52405.1, ECO:0000313|Proteomes:UP000002730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC   {ECO:0000313|Proteomes:UP000002730};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium cellulovorans 743B.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; CP002160; ADL52405.1; -; Genomic_DNA.
DR   RefSeq; WP_010074521.1; NC_014393.1.
DR   AlphaFoldDB; D9SRH6; -.
DR   STRING; 573061.Clocel_2705; -.
DR   KEGG; ccb:Clocel_2705; -.
DR   eggNOG; COG1404; Bacteria.
DR   eggNOG; COG1705; Bacteria.
DR   HOGENOM; CLU_261277_0_0_9; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000002730; 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; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002730};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1198
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003128430"
FT   DOMAIN          158..390
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        167
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        199
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        357
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1198 AA;  132719 MW;  3C7AD534CBB85C53 CRC64;
     MRKRLFGVIV SVFFLISLFS LIHPQSVLAG DSVEKKVNIE NFNADKDTII QNEIVVKYKN
     NQSNSKIFSY FGISRNTESK IEKIKVDNKD QLEQRINELQ NDPNVESIQP NYKYEKFDID
     NTSANNTVHA MTSITGVNDN QWYLERLQIP ELWSQSTGKG IKIAVLDTGI DSNHEDLVGK
     VVGGQDFTGT GSYLDNNGHG TFVAGIIAAD RANNIGISGI AYDSKLLSVK VLNKDGYGDT
     TTISKGIKWA ADNGAKILNL SLGTSKDDAI LKEAVNYAVS KGCIIIASSG NYGLQGITYP
     AAYDNVIAVG AINESTQWCY FSNFGQELDL VAPGSKIYST VPQSINALKY MTYSGTSAST
     AIVSGEVSLL LSKQPQLTVK DILSKIKETS IGIGFYTDEA LLYGNGILDL KKIFTGEYSN
     YSFNRIESRD NNTIDNAERV YNSTAFPYVE LNPHSDVDWY RLDIPEDTVA KITITTPQKN
     IYANIFSDNF YYPDRILKVD GKSEYYISNY YSNRNFYLEL YTPNLEPSNC SLNIQYLSIN
     DPSIPKDQTL KYSIDSISQG KVITGNTLDI SGWALSKLGI TKVEAIVDNQ GFELQYGLSR
     PDVYNAFKDY NDKESGFSSS LNISDIPYGT HSLKLMFTDS RGVISFSNAI TFTTIDTLKY
     SLDTTKSEMT VSGNSLLIAG WALSNASIAK IEAIIDNDNP VALKYGLSRP DVYNAFKGYN
     NKNAGFSSYI NIAKYGYGSH TLQVRLTYVG GRIEILQQIQ FNISGTLKSN LDTLKSNDII
     TGKYINIAGW AISKAGIIKV EAVIYDKAYT LSYGSNRPDV YNAFKDYNNS KAGFSGTIDA
     SKLPIGNYPL YIRITEVGGR VTIDNGRSFR VQNALYCLDT PKAKQLVYGN KLQVSGWALS
     DSGVAKVEML VNDTAKTLNY GISRSDVYNA FPKFNNKNAG FSADIDISKL PYGTIKLKLR
     ITDKLGRVWT QEQVNELEVE IKDTAIFGID TPKDTQSVTG NTLNISGWAL SKSGITKLEV
     LIDDIPYPLT YGISRPDVYN AYKSYNNQSA GFKGTVDISK LDYGYHHLKI RATNRDGRVS
     VSQIHGFGMD STLQYNLETP TYFEKITNGS LNIRGWVLSK FGITKVEALI GDQCYEVQYN
     VSRPDIYNIY KDYKNLNSGF NESLDVSNIP KGSHLLLLRF TDGRGIVNSG PLISVDIQ
//
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