ID   A0A0S1Y7X5_9BORD        Unreviewed;       708 AA.
AC   A0A0S1Y7X5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Metallophosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASB57_27135 {ECO:0000313|EMBL:ALM86136.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM86136.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM86136.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM86136.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP013111; ALM86136.1; -; Genomic_DNA.
DR   RefSeq; WP_057654986.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1Y7X5; -.
DR   STRING; 1746199.ASB57_27135; -.
DR   OrthoDB; 327733at2; -.
DR   Proteomes; UP000064621; Chromosome.
DR   CDD; cd07389; MPP_PhoD; 1.
DR   Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR018946; PhoD-like_MPP.
DR   InterPro; IPR038607; PhoD-like_sf.
DR   InterPro; IPR032093; PhoD_N.
DR   PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   Pfam; PF09423; PhoD; 1.
DR   Pfam; PF16655; PhoD_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT   DOMAIN          54..142
FT                   /note="Phospholipase D N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16655"
FT   DOMAIN          155..665
FT                   /note="PhoD-like phosphatase metallophosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF09423"
FT   REGION          27..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   708 AA;  75868 MW;  3F2838A02E471B14 CRC64;
     MDRRRFLKWS GFISVSVASP VLLTACGGDH DDDDSDTSSP PDTGTTPTGT GFSLGVASGD
     PKPDSVILWT RVDGGSDAAL SVRVQVATDT DFKALVVDTT VSAVAQWDYT VRHKVTGLTA
     NTTYYYRFIS GMATSTTGRT WTAPATDADL ASLKFAFITC QDWNANHWGA FDALVNAEDP
     DIKFIVHVGD YIYERASATR LVPCEDVHPP LVDKLTGGTK VGDDVYATTI GDYRALYKTY
     RSDPRLQALH ARYPFIAIWD DHEFSDDCWG DDSTYNDGSD TSTGVAEPAR RRGANQAWYE
     YMLADVTFTD GLTGDQYLDL QIYRSFTFGK LATLVMTDER LYRADHLISE SLTSGSEIGS
     RYLVPQPLLQ AVEAQKLAGG ALNASVSILG DAQRQWWKDQ MSAANGKTTW KLWGNEVSLM
     RMQVDLVKAL QLGPQLAAGI VTSAPTLAPV QTQLGDAITA DLTAFGKKYL LAKSQGTTLA
     IAASDLTQTQ ALITSLADAT TALGVATGLA TTLNTGYASF FQYFATYLFD CDQWDGYDAE
     RKDLMAYLKT NSIQNVVALT GDLHAIFAGQ VMDDFDAASP TPVMVDLMTP GVSSTSLLGF
     YTAAIKNANH AYDALAGLVL TDVTNYTGDA LSGTVKGANP WIKYVDTNAQ GYAVVTLTPA
     NLTCQIKKVH TLLSDGATAP SGANVVAQVV TATVTAGTPD VTIAVASA
//