ID A0A0Q5T916_9BACT Unreviewed; 508 AA.
AC A0A0Q5T916;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KQS31391.1};
GN ORFNames=ASG33_13830 {ECO:0000313|EMBL:KQS31391.1};
OS Dyadobacter sp. Leaf189.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS31391.1, ECO:0000313|Proteomes:UP000051810};
RN [1] {ECO:0000313|EMBL:KQS31391.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS31391.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS31391.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS31391.1,
RC ECO:0000313|Proteomes:UP000051810};
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.
CC {ECO:0000256|ARBA:ARBA00011073, 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:KQS31391.1}.
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DR EMBL; LMPS01000004; KQS31391.1; -; Genomic_DNA.
DR RefSeq; WP_056285943.1; NZ_LMPS01000004.1.
DR AlphaFoldDB; A0A0Q5T916; -.
DR STRING; 1736295.ASG33_13830; -.
DR OrthoDB; 9792152at2; -.
DR Proteomes; UP000051810; 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 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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF7; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-1 PROTEASE; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051810};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 146..418
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 508 AA; 55493 MW; D8927AAD49AF3437 CRC64;
MKRLLLIAFV LIPVALSASP KYWIYLKNKD LGTSPAVSRQ TLETRQMLGL ALSDETDLPV
RADYEQALKA QSVHIINRSK WLNAVSAVLS SEQAMKVREL DFVKEVVPID PGFYVAKTQP
IEKAQMAPVM SQVQASAFLK EGITAKDVTI GVIDAGFYGA DSSLSLTQIF SNKRILAIRD
YVKPGRPGEL LFSSAESFSD MHGTEVMAAI AGVDFQDEIQ YGMATNAKFY LARTDYSMRE
YRGEEDNWIA AMEWMDSLGV RLINTSLGYA KGFSDPKENY IPSQMDGKTS AISRAAQIAS
DKKGIMLIVS AGNEGDDKSW GIVSAPADAK GVLSVGATNG KLWNRIGYSS VGPEFLSYVK
PNVSCFSLYG TSLSAPVITG FAACLLQANP RLTNKELIAL IEKSSHLYPY GNNFVGYGVP
QASRALALAK APYLPDNAKL VKAKGRSCDV EVTSADSLVA IYRKKTNKDV LSQQVAKVQN
GKVSLKRQNG EHFTTIDLKD NVIEVEWD
//
