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Database: UniProt
Entry: D2UGB5_XANAP
LinkDB: D2UGB5_XANAP
Original site: D2UGB5_XANAP 
ID   D2UGB5_XANAP            Unreviewed;       697 AA.
AC   D2UGB5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   SubName: Full=Putative protease protein {ECO:0000313|EMBL:CBA17426.1};
GN   OrderedLocusNames=XALc_2949 {ECO:0000313|EMBL:CBA17426.1};
OS   Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA17426.1, ECO:0000313|Proteomes:UP000001890};
RN   [1] {ECO:0000313|EMBL:CBA17426.1, ECO:0000313|Proteomes:UP000001890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX   PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA   Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R.,
RA   Cociancich S., Couloux A., Darrasse A., Gouzy J., Jacques M.A.,
RA   Lauber E., Manceau C., Mangenot S., Poussier S., Segurens B.,
RA   Szurek B., Verdier V., Arlat M., Rott P.;
RT   "The complete genome sequence of Xanthomonas albilineans provides new
RT   insights into the reductive genome evolution of the xylem-limited
RT   Xanthomonadaceae.";
RL   BMC Genomics 10:616-616(2009).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
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DR   EMBL; FP565176; CBA17426.1; -; Genomic_DNA.
DR   RefSeq; WP_012917419.1; NC_013722.1.
DR   EnsemblBacteria; CBA17426; CBA17426; XALC_2949.
DR   KEGG; xal:XALC_2949; -.
DR   PATRIC; fig|29447.3.peg.2910; -.
DR   HOGENOM; HOG000159614; -.
DR   OMA; DGKNTTR; -.
DR   OrthoDB; 1281138at2; -.
DR   BioCyc; XALB380358:VB87_RS14850-MONOMER; -.
DR   Proteomes; UP000001890; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00063; FN3; 1.
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; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001890};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW   ECO:0000313|EMBL:CBA17426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    697       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003037121.
FT   DOMAIN      230    602       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   DOMAIN      610    697       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   ACT_SITE    301    301       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    305    305       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    511    511       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       557    557       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       558    558       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       580    580       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       582    582       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   697 AA;  72896 MW;  D47CF6C8DF11BEB1 CRC64;
     MKDVALFRHL PLYIAFFAAL STNAIAASQQ NQTITSELAH LPTQLQSAKK LGALAPSTPI
     NVVMTLPLKD GAGAYDYAMH VSQPGDPLYG HYLTSSQFAK RFGARQSDID AVKAYTQAHG
     MRIKSIGGAG SLITVSAPAD AFSKQLGVNF NRYQDQNGKA FFSADQQPQL PSELVGHVGG
     IVGLHDADRL GTLAIHAPTD PAARAAMNQE RTAHGLRAVP ENIGHGPNGG FSPQDIRKAY
     TIPNQLAPGK SETLAIFAQG GFLSSDIATY EKTFGLPNVP VKVRNVNGYN GAVNYEIVAG
     EIALDIDTAI AVNPQLQQIL IYEEGDDAYP VALLAALGAM ADDNTAQTVS ISYGEDEELM
     GTQALAAEGQ VLTQMVAQGQ GVYASSGDHG AYGRTGSGLH GADPGTQPLV TSVGGTTLFT
     QQDGSYLAEE TWNLLGEQLG ATGGGVSNYW PIPAYQLIPD SNGKQVSIAT PNGGSSTRRN
     FPDVAATGNP ATAIAIYSEL EGGWRIVGGT SLSAPIWASF MTIANQARRY AGLDGIGFAN
     PFLYSNVKGT VSTGTHDILE GSNGIASLFN GVAGFSAGLG YDNTTGLGSM ASWSLLFNSL
     LHGNDRNTPP PGQVRGVSVS TTKTTSTVQW SAAANATGYL ILAYSPTSQI VSYAVTRDTQ
     SMLQGFTPDT TYQFLVVSIN KGGAKVSSKV IAKTAKN
//
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