ID E6WRI4_PSEUU Unreviewed; 490 AA.
AC E6WRI4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADV26715.1};
GN OrderedLocusNames=Psesu_0863 {ECO:0000313|EMBL:ADV26715.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV26715.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV26715.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP002446; ADV26715.1; -; Genomic_DNA.
DR RefSeq; WP_013534545.1; NC_014924.1.
DR AlphaFoldDB; E6WRI4; -.
DR STRING; 743721.Psesu_0863; -.
DR KEGG; psu:Psesu_0863; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_7_6; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000008632; Chromosome.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 181..439
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 469..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 402
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 490 AA; 51045 MW; D8C6B9DBF846CAEB CRC64;
MNATYARGLL PDAVRGRLLL TLRLGEMPAH IPGWRACTHH GTPMAERIDG GVIDRLLRHH
GGAVRAVRLH SARTPRAEHA VAGAYRFDEV EQISGVARVL RIQVREPEGV PALLRALAEL
PMVERVGASR LCCLPFASAL DRDDAASRPV VPDEAARAAD AWVRASTRID EALALEAGDP
AVVVGLADTG VALAHAELER RLRAGFDSVD LDPQAVGGLQ LVGDFRRAGN HPQDEVGHGS
GCAGIIAARG EGIAIGAAGA CGLTPVRVLG AALSGGKRVG IGALDNIDAG MKRLIDLGVK
VINMSFGTPE SMLAGDAPLP HEEIVRYALA RGVILVAASG NSGLAEKYYP AAHPGVIAVG
AVEPDLRPAA FSTRGAHVAL CAPGRDILTC DLSGYQRATG TSFAAPHVAA VCALLASRAL
RRAWPLDGAQ VRRILVESAR PFPVDGVTGC GAGCLDAAAA LRRLDEIVDR EQDEDDREPL
PDGVPPALAA
//
