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Database: UniProt
Entry: Q8PP93_XANAC
LinkDB: Q8PP93_XANAC
Original site: Q8PP93_XANAC 
ID   Q8PP93_XANAC            Unreviewed;       585 AA.
AC   Q8PP93;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   SubName: Full=Protease {ECO:0000313|EMBL:AAM35683.1};
GN   Name=xcp {ECO:0000313|EMBL:AAM35683.1};
GN   OrderedLocusNames=XAC0795 {ECO:0000313|EMBL:AAM35683.1};
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486 {ECO:0000313|EMBL:AAM35683.1, ECO:0000313|Proteomes:UP000000576};
RN   [1] {ECO:0000313|EMBL:AAM35683.1, ECO:0000313|Proteomes:UP000000576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306 {ECO:0000313|EMBL:AAM35683.1,
RC   ECO:0000313|Proteomes:UP000000576};
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F.Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A.Jr., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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; AE008923; AAM35683.1; -; Genomic_DNA.
DR   STRING; 190486.XAC0795; -.
DR   EnsemblBacteria; AAM35683; AAM35683; XAC0795.
DR   KEGG; xac:XAC0795; -.
DR   eggNOG; ENOG4106MUH; Bacteria.
DR   eggNOG; COG4934; LUCA.
DR   HOGENOM; HOG000131438; -.
DR   OMA; TTTWAGE; -.
DR   BioCyc; XAXO190486:XAC_RS04095-MONOMER; -.
DR   Proteomes; UP000000576; 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; cd04056; Peptidases_S53; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000576};
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:AAM35683.1};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    585       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004314818.
FT   DOMAIN      207    583       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    283    283       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    287    287       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    501    501       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       543    543       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       544    544       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       561    561       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       563    563       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   585 AA;  61073 MW;  A29B8127936CA653 CRC64;
     MVTRSFSHAV LACAVALGMI GIAPAAEQAP AQLAVGGALA PQRILQVGLV LKPQVAMRQQ
     HAAVEQWLMR DGGDPLLRGQ LARASAASTS QIAQVKAYLS RYGITDVRPA TDGRLLQVRA
     TAAALQAALG TPLRVVSADG RVGIAAAQGA VAVPAGLQAV VQGVVGLDGT AGAKVAPHGA
     PLSAARTSLS NSSAVVAANS GGAEVVRHSI EELNSAYGAD TLAPASDIVG AVIAAGNLEQ
     TLVRLQSFQA LHGLHTPVTV VTVGEPGAPG YQSNAASKDS EVEWDMDTQL LVGSAGGLKR
     LIIYNIPDFS WNSMIDGMAR AADDNLARVV SMSIYGQEIQ VDDAVFQAMD ASLTKAVRQG
     QNFVICSGDD GVYLPLSARA NAPYYDTLAG RPDLRQVGWP ASHRYAIAVG ATELLTQGGN
     PGSYASERVW NAGVGRQLSQ GGVSKIAYAP QWQRTLLPGQ TASGYRAVPD VSFNGSFYSS
     AQIRGTDAQG NEAAWYVWGT SAATPTFAGY IARLLQSHPN LGFVAPQIYQ YASQRHDAQR
     AHDVVVGSNG LYRDGYNASY GWDFASGWGS MNIGDFDRFL TQASP
//
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