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-APR-2013, entry version 81.
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.
OX NCBI_TaxID=136420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=8902622;
RA Oda K., Ito M., Uchida K., Shibano Y., Fukuhara K., Takahashi S.;
RT "Cloning and expression of an isovaleryl pepstatin-insensitive
RT carboxyl 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
RP 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
RT carboxyl proteinases from prokaryotes by site-directed mutagenesis.";
RL J. Biol. Chem. 274:27815-27822(1999).
CC -!- CATALYTIC ACTIVITY: Cleavage of casein.
CC -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Autocatalytically processed.
CC -!- SIMILARITY: Belongs to the peptidase S53 family.
CC -!- SIMILARITY: Contains 1 PKD domain.
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DR EMBL; D83740; BAA12093.1; -; Genomic_DNA.
DR ProteinModelPortal; Q60106; -.
DR SMR; Q60106; 241-625.
DR MEROPS; S53.002; -.
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 Gene3D; 2.60.40.670; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR015366; Peptidase_S53_propep.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR009020; Prot_inh_propept.
DR Pfam; PF00801; PKD; 1.
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; SSF52743; Pept_S8_S53; 1.
DR SUPFAM; SSF49299; PKD; 1.
DR SUPFAM; SSF54897; Prot_inh_propept; 1.
DR PROSITE; PS50093; PKD; 1.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Metal-binding; Protease; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1 23 Potential.
FT PROPEP 24 237 Removed in mature form.
FT /FTId=PRO_0000027365.
FT CHAIN 238 635 Xanthomonalisin.
FT /FTId=PRO_0000027366.
FT PROPEP 636 827 Removed in mature form.
FT /FTId=PRO_0000027367.
FT DOMAIN 635 722 PKD.
FT ACT_SITE 312 312 Charge relay system (By similarity).
FT ACT_SITE 316 316 Charge relay system (By similarity).
FT ACT_SITE 544 544 Charge relay system (By similarity).
FT METAL 585 585 Calcium (By similarity).
FT METAL 586 586 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 603 603 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 605 605 Calcium (By similarity).
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
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