ID A0A0Q9T8H4_9BACL Unreviewed; 387 AA.
AC A0A0Q9T8H4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:KRF31984.1};
GN ORFNames=ASG93_06595 {ECO:0000313|EMBL:KRF31984.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF31984.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF31984.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF31984.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF31984.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF31984.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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:KRF31984.1}.
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DR EMBL; LMSP01000012; KRF31984.1; -; Genomic_DNA.
DR RefSeq; WP_056833008.1; NZ_LMSP01000012.1.
DR AlphaFoldDB; A0A0Q9T8H4; -.
DR STRING; 1736411.ASG93_06595; -.
DR OrthoDB; 9002785at2; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04056; Peptidases_S53; 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; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..387
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006384158"
FT DOMAIN 51..386
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 387 AA; 40508 MW; 39D944494F0E6386 CRC64;
MKKWLQYFSV LACAFLCFLC IVGFSSAAPL QDAHPPIHIK NNGATPNYQN GFAPAQIKKM
YGLDRLSSTY TGAGQTIAII DAYGSPTIVN DLQVFNTQFG LPPADLTIAY PNGKPNKADG
GWALETSLDV EWAHAVAPQA KILLVVAKSA TLSNLLAAVD YATSHGAQVV SNSWGGSEFS
SEASYDSHFQ RSGVVYVASS GDNGSGMSWP ASSPYVLSVG GTTLNADSTG SYVSESGWSG
SGGGASSYES RPSYEDIWQT VVGSYRGSPD VSWDADPNTG VAVYDSTSYS GQKGWFQVGG
TSFGAPCWAA MIALADQGRS TPLTNYNAIA NLYSIAGATD SLGYTNDYHD INKGSNGGYS
AQAGYDLVTG IGSPKADLLI PALNKSK
//
