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Database: UniProt
Entry: Q60106
LinkDB: Q60106
Original site: Q60106 
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   22-JAN-2014, entry version 83.
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: Contains 1 peptidase S53 domain.
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; SSF49299; SSF49299; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   SUPFAM; SSF54897; SSF54897; 1.
DR   PROSITE; PS50093; PKD; 1.
DR   PROSITE; PS51695; SEDOLISIN; 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      241    625       Peptidase S53.
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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