ID W4SI10_9XANT Unreviewed; 436 AA.
AC W4SI10;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:GAE56156.1};
GN ORFNames=XPR_2791 {ECO:0000313|EMBL:GAE56156.1};
OS Xanthomonas arboricola pv. pruni MAFF 301420.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1418095 {ECO:0000313|EMBL:GAE56156.1, ECO:0000313|Proteomes:UP000019084};
RN [1] {ECO:0000313|EMBL:GAE56156.1, ECO:0000313|Proteomes:UP000019084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 301420 {ECO:0000313|Proteomes:UP000019084};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) 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:GAE56156.1}.
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DR EMBL; BAVC01000237; GAE56156.1; -; Genomic_DNA.
DR AlphaFoldDB; W4SI10; -.
DR Proteomes; UP000019084; 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; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..436
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004848567"
FT DOMAIN 185..415
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 227
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 377
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 436 AA; 44869 MW; 700FA0475F40591C CRC64;
MKRLLAIGII AACIGLGPHA AAQEPAQAAA SASTPPAADA HTPDSSRDIL LAVANPLSAP
PARAGSSLIG YASSYYGAGQ KAAVRMEALK QRYKLREVSG WPITSLGLYC AVLQPPPGVS
RDELVSALAD DDGVELVQPV QDFSVFSADA SEKTTALSGY NDPYVDLQRG FIATDAASAQ
TVTQGRGVVV AVVDTGVDTT HADLKARIRD VHDLVDDSPV MTSSDSHGTE VAGIIAAGSN
NHQGIVGMAP KAMLSIYKAC WYAPTVGATA RCNTFTLAKA LAAINNSSAR VINLSLGGPA
DPLLSKMLQH LVQQGRIVVA AMPPNGRLDG FPNDVPGVLV VRSSSPTAAM PGVLSAPGKD
ILTTQPNGRY DFTSGSSMAT AHVSGVVALL LSLSPSLDAT ALRELMQRTS KLSDGQLQIN
AGAAVQALAP PARHSN
//
