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Database: UniProt
Entry: H8L2U6_FRAAD
LinkDB: H8L2U6_FRAAD
Original site: H8L2U6_FRAAD 
ID   H8L2U6_FRAAD            Unreviewed;       596 AA.
AC   H8L2U6;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   08-MAY-2019, entry version 36.
DE   SubName: Full=Putative protease {ECO:0000313|EMBL:AFC87302.1};
GN   OrderedLocusNames=Fraau_2972 {ECO:0000313|EMBL:AFC87302.1};
OS   Frateuria aurantia (strain ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB
OS   13370) (Acetobacter aurantius).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Frateuria.
OX   NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC87302.1, ECO:0000313|Proteomes:UP000005234};
RN   [1] {ECO:0000313|Proteomes:UP000005234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB 13370
RC   {ECO:0000313|Proteomes:UP000005234};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G.,
RA   Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Frateuria aurantia DSM 6220.";
RL   Submitted (FEB-2012) 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; CP003350; AFC87302.1; -; Genomic_DNA.
DR   RefSeq; WP_014404305.1; NC_017033.1.
DR   STRING; 767434.Fraau_2972; -.
DR   EnsemblBacteria; AFC87302; AFC87302; Fraau_2972.
DR   KEGG; fau:Fraau_2972; -.
DR   KO; K05999; -.
DR   OMA; TTTWAGE; -.
DR   OrthoDB; 1281138at2; -.
DR   BioCyc; FAUR767434:G1H2L-2951-MONOMER; -.
DR   Proteomes; UP000005234; 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   CDD; cd11377; Pro-peptidase_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:UP000005234};
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:AFC87302.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005234};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    596       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003614168.
FT   DOMAIN      229    594       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    303    303       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    307    307       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    513    513       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       554    554       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       555    555       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       572    572       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       574    574       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   596 AA;  62658 MW;  44318D8493329BC7 CRC64;
     MNRKIAPLLR RPLGVILPLL LGLTAHSAFA ADDWAPTATK AFVPTLLRAP ASPGSSTARL
     QASLRSASSH AVKLASDDIR DIDVVVSLKP RDEAGLDQWL AQRLDQRPLP ALGRDELIRR
     HAPSQAQVDA VVAHLKAAGF NRIQVAPNRL LIEASGRAGA VENAFHTGLN HFQYQGRDVI
     TNTEDAEVPQ ALAGTVQAVL GLQTAVQAHT LHHVVKPAGS GARPDASGST FSHQLTDFPG
     IYHAEGLPKG TDTTVAIITA YDLSDTLANL RHFAADHQLT VPTTQVIKTS TGNYANNGDA
     TGEWSLDSQA IVAVSGGLKT LQFFNAQDLS DAALLKAYNA AVNDGSAKAV NVSLGLDEAV
     THADGSQASE DAIFKLAAAQ GQTFSISSGD EGVYEAEGGY IRAITDPASY TVSDPATSPW
     VLAVGGTEVA TSGNTGYVGE ITWNEGVDWF GRLWSTGGGI SKYETAPAWQ TRYLGNRLTT
     GQRVLPDFSF DASGASGAQV YVDGSYINVG GTSLAAPIFA GLWARLQTAN RNNLGFAATE
     LYPLASANPT VLHDVVSGNN GYNGYGYQAG PGWDYPTGWG SFDTAGIQSL LQQAAR
//
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