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Database: UniProt
Entry: A0A1A9N072_9BURK
LinkDB: A0A1A9N072_9BURK
Original site: A0A1A9N072_9BURK 
ID   A0A1A9N072_9BURK        Unreviewed;       519 AA.
AC   A0A1A9N072;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   05-JUN-2019, entry version 14.
DE   SubName: Full=Peptidase S53 {ECO:0000313|EMBL:OAJ54691.1};
GN   ORFNames=A6V37_34150 {ECO:0000313|EMBL:OAJ54691.1};
OS   Paraburkholderia ginsengiterrae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1462993 {ECO:0000313|EMBL:OAJ54691.1, ECO:0000313|Proteomes:UP000078116};
RN   [1] {ECO:0000313|EMBL:OAJ54691.1, ECO:0000313|Proteomes:UP000078116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCY85 {ECO:0000313|EMBL:OAJ54691.1,
RC   ECO:0000313|Proteomes:UP000078116};
RA   Dobritsa A.P., Kutumbaka K., Samadpour M.;
RT   "Reclassification of Paraburkholderia panaciterrae (Farh et al. 2015)
RT   Dobritsa & Samadpour 2016 as a later homotypic synonym of
RT   Paraburkholderia ginsengiterrae (Farh et al. 2015) Dobritsa &
RT   Samadpour 2016.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAJ54691.1}.
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DR   EMBL; LXKA01000347; OAJ54691.1; -; Genomic_DNA.
DR   RefSeq; WP_064265679.1; NZ_LXKA01000347.1.
DR   EnsemblBacteria; OAJ54691; OAJ54691; A6V37_34150.
DR   Proteomes; UP000078116; Unassembled WGS sequence.
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   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078116};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078116};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   DOMAIN      177    519       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   REGION        1     20       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1A9N072}.
FT   REGION      229    249       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1A9N072}.
FT   COMPBIAS    230    244       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1A9N072}.
FT   ACT_SITE    249    249       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    253    253       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    449    449       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       486    486       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       487    487       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       500    500       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       502    502       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   519 AA;  52825 MW;  612E30C8A5EF9733 CRC64;
     MVNKHPLPGS ERTVEAGSKV VGQCDPAERI EVFVMLRRQQ QAQFDALMSK IEAGDPSVKP
     LSREALAQDY GAAPDDVVKV KSFAAAHGLT VLREDPAART VVLGGTIAQF QTAFGVKLEH
     YEHHITGQFR GRTGTISVPD DLHGVVQAVL GLDNRPQARP HFRIRPPFQP ARGRQVSFTP
     PQIASLYNFP QGDGSGECVG IIELGGGYNT SDLKAYFGSL GVAEPTVKSV GVDQGSNQPS
     GDPNGPDGEV TLDIEIVGAI VPGAAIAVYF TPNSDAGFID AVSRAVHDTA NKPSVISISW
     GGPESNWTSQ SVQAFNSVLQ SAAALGVTVC AASGDSGSSD GTGGGDQVDF PASSPYVLAC
     GGTHLSASGT SISSEVVWND GAQGGASGGG VSRAFPVPAW QEGLTVTSSS GSGTALSGRG
     VPDVAGDASP TTGYTVLIDG TQTVVGGTSA VAPLWAALIA RINAAKGQPA GFINAKLYKA
     AGACNDITQG NNGSFAASVG WDACTGLGSP NGQKVAAAL
//
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