ID   A0A1Y6HFB8_9XANT        Unreviewed;       628 AA.
AC   A0A1Y6HFB8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:SMR02219.1};
GN   ORFNames=PD5205_00900 {ECO:0000313|EMBL:SMR02219.1};
OS   Xanthomonas fragariae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=48664 {ECO:0000313|EMBL:SMR02219.1, ECO:0000313|Proteomes:UP000195953};
RN   [1] {ECO:0000313|EMBL:SMR02219.1, ECO:0000313|Proteomes:UP000195953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD5205 {ECO:0000313|EMBL:SMR02219.1};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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       ECO:0000256|RuleBase:RU003355}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT853885; SMR02219.1; -; Genomic_DNA.
DR   RefSeq; WP_002811980.1; NZ_ORZY01000054.1.
DR   AlphaFoldDB; A0A1Y6HFB8; -.
DR   STRING; 48664.BER92_04350; -.
DR   KEGG; xfr:BER92_04350; -.
DR   eggNOG; COG1404; Bacteria.
DR   OrthoDB; 9790784at2; -.
DR   Proteomes; UP000195953; Chromosome 1.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07496; Peptidases_S8_13; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034176; Peptidases_S8_13.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF04151; PPC; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..628
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011001306"
FT   DOMAIN          191..486
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          549..613
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        263
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        447
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   628 AA;  64023 MW;  B93759F1634078C8 CRC64;
     MIDKNFRLKP LAGAILMMAL SASGTLAAAP GLLVKEPTQA VPASAASSSR LIVRYKDNTV
     AATDRASKLS TVQAAVGRVG ASSGARASAA AAKATYVRKL GIGSDLIKLS STLTAAQVNK
     VVVELRNDPS VADVHIDRML HPVDIDIKHL AATDVSSQLV PNDPLYAQRQ WHLSNPNGGI
     NAPAAWDLSQ GAGVVVAVLD TGILPDHPDF AGNLLQGYDF ITDAEVSRRP TDARVPGALD
     YGDWQEADNV CYGGSVAQGS SWHGTHVSGT IAEATNNGLG MAGVAPKATI LPVRVLGRCG
     GYTSDIVDAI VWASGGTVEG VPANINPAEV INMSLAGGEA CDSATQLAIN DAVSRGTTVV
     VSAGNGSEDV ANYSPASCDN TITVGATRIT GGIAYYSNYG SKVDLSGPGG GGSVDGTPGG
     YIWQAGYTGA TTPTSGKYDY MGLGGTSMAS PHVAGVVALV QSASIGLGDG PLTPAAVDAL
     LKQTSRHFTV TPMASTPVGS GIVDAKAALE AVLVEPCDPA TESCAPPAIA LTNKVPVTDL
     SGAYASSMLY SFEAKAGAVL SFMTYGGSGD VSVYVSFGAE PSATSYDAKS TRRGNSETVR
     FTAPKAGTYY IKLMGVKDYA KLTLVARQ
//