ID A0A117LWW7_9FIRM Unreviewed; 620 AA.
AC A0A117LWW7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:KUK72040.1};
GN ORFNames=XD91_1568 {ECO:0000313|EMBL:KUK72040.1};
OS Clostridiales bacterium 38_11.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1641393 {ECO:0000313|EMBL:KUK72040.1, ECO:0000313|Proteomes:UP000053314};
RN [1] {ECO:0000313|Proteomes:UP000053314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK72040.1}.
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DR EMBL; LGGM01000086; KUK72040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LWW7; -.
DR PATRIC; fig|1641393.3.peg.634; -.
DR Proteomes; UP000053314; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 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; IPR034084; Thermitase-like_dom.
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; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 159..406
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 620 AA; 68247 MW; 8AC51DFC8320FBCA CRC64;
MRAMLLKKSS LLLTILMLST TLFGCAVGTT RSRGLEEAGA NKLIVELENG QKISEIEKIL
GNVNIAQLQG GRYIISSNDS EEELEQRLSA MKGIRRIQKP RNIGIIRPIT KIKVGKDFII
DNLSQTNDIE ANDPGVKSQW AVSYTNANHV WPLVEQKETI YVAIVDTGVD YTHPDLKNRV
DLGKGYDFIN NDSDPMDDNG HGTHISGIIA AEMNNGEGIV GVAGTLDVRI IPIKVLDSEG
YGQSDIVAKG IEYAVDQGAN IINLSLGGPG EDVDIANAVR YASEKGVLVV AASGNDNQNS
DSYTPAGLEN VYTVGAINPL KTKARFSNYG NSVEAVAPGV KILSAVPGNQ YEAWDGTSMA
APVVSGIASI MLAQKPDIDV DELVAILNES AEDILEEGKD QKSGYGLPNA EKAWQLLTGE
ETPPAEEEAM YNSLQEAIGA ASKLKIQQND VNSLMVSSNN TDSGSERRSE LSDLIEEGSK
YKEENEEQIV EWKKEFKENQ EINKQYMQEI YEGLKTLKPL LEQFQDGYKQ GALELTSKEL
NQIQQEIEKL ESYQAYVKTR SEERQKMWDE MAQMFSEGNY EEAMAMFPDI LEAQKALTKN
LELLLNEINE LTKLFEGVLD
//
