ID   XANP_XANS2              Reviewed;         827 AA.
AC   Q60106;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Xanthomonalisin;
DE            EC=3.4.21.101;
DE   AltName: Full=Carboxyl proteinase;
DE   AltName: Full=XCP;
DE   AltName: Full=Xanthomonapepsin;
DE   AltName: Full=Xanthomonas aspartic proteinase;
DE   Flags: Precursor;
OS   Xanthomonas sp. (strain T-22).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas; unclassified Xanthomonas.
OX   NCBI_TaxID=136420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=8902622; DOI=10.1093/oxfordjournals.jbchem.a021451;
RA   Oda K., Ito M., Uchida K., Shibano Y., Fukuhara K., Takahashi S.;
RT   "Cloning and expression of an isovaleryl pepstatin-insensitive carboxyl
RT   proteinase gene from Xanthomonas sp. T-22.";
RL   J. Biochem. 120:564-572(1996).
RN   [2]
RP   MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES, AND ACTIVE SITES.
RX   PubMed=10488127; DOI=10.1074/jbc.274.39.27815;
RA   Oyama H., Abe S., Ushiyama S., Takahashi S., Oda K.;
RT   "Identification of catalytic residues of pepstatin-insensitive carboxyl
RT   proteinases from prokaryotes by site-directed mutagenesis.";
RL   J. Biol. Chem. 274:27815-27822(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of casein.; EC=3.4.21.101;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Autocatalytically processed.
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; D83740; BAA12093.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q60106; -.
DR   SMR; Q60106; -.
DR   MEROPS; S53.002; -.
DR   KEGG; ag:BAA12093; -.
DR   BRENDA; 3.4.21.101; 6720.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF04151; PPC; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00089; PKD; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF49299; SSF49299; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS50093; PKD; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Hydrolase; Metal-binding; Protease; Secreted; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..237
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000027365"
FT   CHAIN           238..635
FT                   /note="Xanthomonalisin"
FT                   /id="PRO_0000027366"
FT   PROPEP          636..827
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000027367"
FT   DOMAIN          241..625
FT                   /note="Peptidase S53"
FT   DOMAIN          635..722
FT                   /note="PKD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT   ACT_SITE        312
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        316
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        544
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         585
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         586
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         603
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         605
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   827 AA;  83707 MW;  21A33C4C683DBC8F CRC64;
     MKIEKTALTV AIALAMSSLS AHAEDAWVST HTQAAMSPPA STQVLAASST SATTTGNAYT
     LNMTGSPRID GAAVTALEAD HPLHVEVALK LRNPDALQTF LAGVTTPGSA LFGKFLTPSQ
     FTERFGPTQS QVDAVVAHLQ QAGFTNIEVA PNRLLISADG TAGAATNGFR TSIKRFSANG
     REFFANDAPA LVPASLGDSV NAVLGLQNVS VKHTLHHVYH PEDVTVPGPN VGTQAAAAVA
     AHHPQDFAAI YGGSSLPAAT NTAVGIITWG SITQTVTDLN SFTSGAGLAT VNSTITKVGS
     GTFANDPDSN GEWSLDSQDI VGIAGGVKQL IFYTSANGDS SSSGITDAGI TASYNRAVTD
     NIAKLINVSL GEDETAAQQS GTQAADDAIF QQAVAQGQTF SIASGDAGVY QWSTDPTSGS
     PGYVANSAGT VKIDLTHYSV SEPASSPYVI QVGGTTLSTS GTTWSGETVW NEGLSAIAPS
     QGDNNQRLWA TGGGVSLYEA APSWQSSVSS STKRVGPDLA FDAASSSGAL IVVNGSTEQV
     GGTSLASPLF VGAFARIESA ANNAIGFPAS KFYQAFPTQT SLLHDVTSGN NGYQSHGYTA
     ATGFDEATGF GSFDIGKLNT YAQANWVTGG GGGSTNAPPV ANFSVATTGL VATFTDSSTD
     SDGSIASHAW TFGDGSTSTA TSPSHTYSAA GTYSVAETVT DNAGATSTKT SSVTVSSSGG
     TGGGTVLQNG VAATGLSAAK NGQLKYTVAI PSGAKSLKIA ISGGTGDADL YVKFGSAPTT
     SSYDCRPYVT GNTESCSFAS PQTGTYYVLL NGYAAFSGVS LKATWTN