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
//