ID A0A0Q5STK0_9BACT Unreviewed; 1776 AA.
AC A0A0Q5STK0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peptidase S8/S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:KQS26643.1};
GN ORFNames=ASG33_18915 {ECO:0000313|EMBL:KQS26643.1};
OS Dyadobacter sp. Leaf189.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS26643.1, ECO:0000313|Proteomes:UP000051810};
RN [1] {ECO:0000313|EMBL:KQS26643.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS26643.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS26643.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS26643.1,
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. {ECO:0000256|PROSITE-
CC 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:KQS26643.1}.
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DR EMBL; LMPS01000006; KQS26643.1; -; Genomic_DNA.
DR RefSeq; WP_056288956.1; NZ_LMPS01000006.1.
DR STRING; 1736295.ASG33_18915; -.
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 CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
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 InterPro; IPR026444; Secre_tail.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF07705; CARDB; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1776
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006262105"
FT DOMAIN 266..500
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1146..1221
FT /note="CARDB"
FT /evidence="ECO:0000259|Pfam:PF07705"
FT DOMAIN 1699..1769
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
FT REGION 1268..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 249
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 446
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1776 AA; 195262 MW; 59EF352BA6F74384 CRC64;
MTSKTRTACL VILLLVSSTS IFAQHLAQRQ LFLKNRVLSL SAGIPDEMGF NNRRLQEQEN
GKFLMIIQFD SIPGETVLSY LKSNGIEVLD YIPDYAYTTT VTARINREVL EKAGVRAIFR
LGIEDILHPL LQPGFIPEHA KKVAGKADVT LSFARSFTFD EVIRDIQKSG FEVLSDKLKS
YQLLEVRVSE DSLQHLAAFP WVQYLAPVQP PSEMLNDKST ASTKANVLGS TALLGYQLTG
EGVVLGLGDD SNPLLHPDIG RRVINYDMLN NTWHGIHVGG IAAGSGLLNE KYKGYAPQSK
IVFRRRSDIV FNAPEFVRDY GMVVTSNTYP GGSGCGTFGT YTYDSPILDQ QAFELPHLQH
IFAAGNSGME TNCQVSPAGY GTVLGTFQSA KNVLTVGMTQ ANLLINPTSS KGPVADGRIK
PEITAPGSAI FSTIPGNTYQ SASGTSMATP AVTGGAALLY QRYRQLNQGQ NPKNALMKAL
ITNGASDQGL PGPDYTYGFG LMNLLRSVTI LDKGHFFSGT VTHAVTNTHQ IVVPANTAKL
KVLIYWNDPA PSVLAGGSAL VNNLDLSVIR PDNTKMRPVF PSAADPTAAA KSGIDSLNNI
EQIFVDAPAP GTYTVEVAAT RIPQGVQEYF IVYDVIEPSL TLTYPLAGEH LTKGDALNIC
WESYGDATST FKVSYSLNDG AAWTTLNANV AADQRQLPWT VPDAATGKAK VKIERNGSSN
VSGAFAIIGV PSVTLQSAQC EGYIALQWNA VNGASDYEVM FSLGGEMKSA AITNALKYTL
SGLSLDSVYY VSVRARKDQV PGRRSFAVIR KPDSGTCAGS ISDNNLKLEA VLSPLPNARK
FTYAAYLPEH SIQIRIKNLD DQPQAGPYEV GYSLGGAMHW ETVNTPLAAL ASADYTFQKK
ADLASLHEGT LLVRLRLAGD PVQENDSLAI GLRQLPNPKV VLPYVHHAGS LPAMDVRETR
MALQGAGEYD FIRVNGEGRL RTADSSKIWS STQVAFILDK TRNDTEKVRS YLEGTYNLSD
YHVQDDEVRL TFRHQYSYSY YHDFNRVYIR GGGNDPWILA YVRDAGTYGE FEDWFKLVSV
DVTPLLRTNG QDFSAGFQVR WAAEAFNTYP EDGFIVDNIK LFKTTSDVEL VRLHVPPVSP
CESAAPASLD VVLRNNGSDN NVNVPVKMSV DGKVSEHTID IIRKGDSTVV RLYYPTEIYT
SGKHLVRVWS DKGSDINRAN DTLEVELFTA ATISIDNTHL ENFELGNGGW FTEGDHSLWQ
FVTPEATGES VAGSGNNAWK TDPEGAGSNS ESYLYSPCFN MNSYPLHLSF SAKIDMEDCD
GNACDMLYLE YNSGYGWYRV GTNGDGTNWY NQQKDGLGHW SGKVATGWRV FTTTLPYQSN
LRLRFVIKTN SNVAKRNIVI DDVHIYSMPY HIYDGSSSTF DMGPSYLSNG GWVPYFINDK
IAMAIEPRGQ NTERIGLNTY FNEGALQFSK DQLILDRNWV INTDADLDNP VGVRLYLPET
TIERLVTDTA YPDLVKPASV YDLSLTKYAG PNQDGDLGNN ANEGWDYFPA DKVKKVPYRN
GYYLEFETKT FSEFWLAKSY IGTGTPLPAE LISFTAEKIH SGEHTAVQLK WATAEEKAFG
HFVVQVAVGS ENAKKGLFAD LGIVKGKAMP GVQQYAFADD KSTLNNTHYY RLKMVDVDGS
FEFSSVRAVI FNTSTAWRIF PNPSRDIFRL EPQGVVKGPV EIEVIDLSGK VRKQMKFREV
TSALDIQLGT PDLPGGLYLL NVKSNEGEVR LRVMKE
//
