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Database: UniProt
Entry: A0A1I6K2L9_9GAMM
LinkDB: A0A1I6K2L9_9GAMM
Original site: A0A1I6K2L9_9GAMM 
ID   A0A1I6K2L9_9GAMM        Unreviewed;       881 AA.
AC   A0A1I6K2L9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   28-FEB-2018, entry version 4.
DE   SubName: Full=Xanthomonalisin {ECO:0000313|EMBL:SFR85492.1};
GN   ORFNames=SAMN05216570_0026 {ECO:0000313|EMBL:SFR85492.1};
OS   Dyella sp. OK004.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1855292 {ECO:0000313|EMBL:SFR85492.1, ECO:0000313|Proteomes:UP000198834};
RN   [1] {ECO:0000313|EMBL:SFR85492.1, ECO:0000313|Proteomes:UP000198834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK004 {ECO:0000313|EMBL:SFR85492.1,
RC   ECO:0000313|Proteomes:UP000198834};
RA   de Groot N.N.;
RL   Submitted (OCT-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};
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DR   EMBL; FOZI01000001; SFR85492.1; -; Genomic_DNA.
DR   Proteomes; UP000198834; 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; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00801; PKD; 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   PROSITE; PS50093; PKD; 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:UP000198834};
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:UP000198834};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     34       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        35    881       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011476679.
FT   DOMAIN      251    628       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   DOMAIN      636    722       PKD. {ECO:0000259|PROSITE:PS50093}.
FT   ACT_SITE    322    322       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    326    326       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    547    547       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       588    588       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       589    589       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       606    606       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       608    608       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   881 AA;  91091 MW;  B622B707DCE6E936 CRC64;
     MTSRKTKWGV AKGHRKALLP LAVSMAMLAG TTQAATDSWV NTNTHAAMQK SAAPAGTASV
     STMAAGQAWT LTMRGNPTVA DTLVTPLEQS KPLHVAVSLK LRNESQLQQL LHELATPGSA
     HYGKFLTPAQ FKANYAPTEQ QVQAVIAHLR SAGFTNITVA PNNLLVEADG NAGSVQAGFR
     TTMKQFEFRG RQRIANDGEV LVPAALGDTV NAVLGLQDVS VKHTMYHFIK PNTSSELHSN
     VTTQATGSIT SHNPTQFASI YDAGTTPNAS NTTVGVITWG DTTQTISDLN TFTSNAGLPT
     TNVQTVKVGT AALWDDANGD GEWDLDTQTI VGTSGGVQKL ILYTAANGTN NGSLTDAGIT
     AAYNKAVTDN VAKVINVSLG EDETASHNAG TQAADDNVFQ QAVAQGQTFS ISSGDEGVYE
     SQGGVLTNSS GTVTANLSSY SVSEPATSPY VVAVGGTTLS TTNGNVWAGE TVWNEGLAQV
     SSTDTRKRLW ATGGGVSSFE NAPAWQTTAL GSSVTKRVLP DVAFDAAQSS GAQIVYQGSV
     AQIGGTSLAS PIFVGVWSRI QSANSNNLPF PTSKMYADFP NHPELLHDVT SGNNGYNGYG
     YNAAAGWDYT TGWGSLDIAK LNTFAAANWV SGGGGTGGTP TANFSFTTSG LTANFTDSST
     DSGGSISSHS WTFGDGSSST ATSPSHAYAA AGTYSVTETV TDGVSAKTSS KTASVTVSSG
     GGATQLLGNT GFESGAASPW SISSGALCSN STCSGQTAHA GSWFVWLDGY GSSHTDTLSQ
     QVAITAGKTS ASLTFYLHID TAETTTTTAY DKLNVQVLNS SGTVLKTLAT YSNLNAASGY
     ALRTFDLSAY IGQTVTIKFT GTEDSSLQTS FVVDDVNLNV Q
//
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