ID C5D8E4_GEOSW Unreviewed; 640 AA.
AC C5D8E4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ACS25782.1};
GN OrderedLocusNames=GWCH70_3123 {ECO:0000313|EMBL:ACS25782.1};
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS25782.1};
RN [1] {ECO:0000313|EMBL:ACS25782.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS25782.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP001638; ACS25782.1; -; Genomic_DNA.
DR AlphaFoldDB; C5D8E4; -.
DR STRING; 471223.GWCH70_3123; -.
DR MEROPS; S08.126; -.
DR KEGG; gwc:GWCH70_3123; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_7_9; -.
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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
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; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR001119; SLH_dom.
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 Pfam; PF00395; SLH; 3.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51272; SLH; 3.
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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..640
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002950341"
FT DOMAIN 463..522
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 523..586
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 587..640
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 640 AA; 69653 MW; 54C4C1EA5188DD5F CRC64;
MMKKWCLVFF SVVLAMMSFL PVASTFAAET KRVNVIILFK KHADEKTVEQ LQGKVYRQFE
VIPALSANVP LASIDILRQL PEVEYVQQDE TVAIDGQVAD WGVKKTKATD MHARGVTGKG
VKIAILDTGI DTKHPDLRVS GGACMLSYCP NSYNDDNGHG THVAGIIAAK NNRIGVLGVA
PEASIYAVKV LNRFGEGTVS TVLAGIEWAI QNHMDIINLS LATPEGSPVL KEAIDKAYQK
GILIVAAAGN NGNRNGIGDT VEYPAKYDSV IGVSAVNKNN VRIAYSATGP AVEVAAPGED
IYSTVPVAYD SDSNPDGYTW MSGTSMAAPF VSGILALYKQ QYPDKTNVEL RQMLRANALD
LGAPGKDNWY GYGLVQAKPN KPPQLEVKLQ SNAAGVVNFS VTPLADNIKG YNVYRNGKQI
KELQTSSSFT DYVLKGNYRY QFSSVYSDGT ESALSNPMTV TVSAPDYKDL TNDIWYAPPI
IYLSSRGIVT GYNNGTIKPN DFVTRAEAVA MLGRALHLDS TKRPTVFKDV DPANFASGYI
QSAYEKGWLN GFPDGTFRPK QPITRAETAI LLAKAYQFPS APSLAFKDVT DKVTGHKEIY
KVAAAKITKG YPDGTFKPYQ SVKRLEFFVF IARAENDAFK
//
