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Database: UniProt
Entry: A0A0A8JPI0_BACSX
LinkDB: A0A0A8JPI0_BACSX
Original site: A0A0A8JPI0_BACSX 
ID   A0A0A8JPI0_BACSX        Unreviewed;       165 AA.
AC   A0A0A8JPI0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU362039};
GN   ORFNames=OXB_3190 {ECO:0000313|EMBL:BAQ11659.1};
OS   Bacillus sp. (strain OxB-1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ11659.1, ECO:0000313|Proteomes:UP000031651};
RN   [1] {ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAQ11659.1, ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ11659.1,
RC   ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL   Genome Announc. 3:e00025-15(2015).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|RuleBase:RU362039};
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. YfcE
CC       family. {ECO:0000256|ARBA:ARBA00008950, ECO:0000256|RuleBase:RU362039}.
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DR   EMBL; AP013294; BAQ11659.1; -; Genomic_DNA.
DR   RefSeq; WP_041075401.1; NZ_AP013294.1.
DR   AlphaFoldDB; A0A0A8JPI0; -.
DR   STRING; 98228.OXB_3190; -.
DR   KEGG; baco:OXB_3190; -.
DR   HOGENOM; CLU_063749_2_0_9; -.
DR   OrthoDB; 9800565at2; -.
DR   Proteomes; UP000031651; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00841; MPP_YfcE; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041802; MPP_YfcE.
DR   InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR   NCBIfam; TIGR00040; yfcE; 1.
DR   PANTHER; PTHR11124:SF12; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 29; 1.
DR   PANTHER; PTHR11124; VACUOLAR SORTING PROTEIN VPS29; 1.
DR   Pfam; PF12850; Metallophos_2; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU362039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031651}.
FT   DOMAIN          1..142
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF12850"
SQ   SEQUENCE   165 AA;  18312 MW;  E5329368B4AC99FD CRC64;
     MKIIVMSDSH GDQETVKAVS SLSGDATFHC GDSELSFDDP LLENIHTVRG NCDLDSRFPS
     SVLVEVGNKK VLAVHGHEHD VKRSLMMLYY TAKEQGADIV LFGHSHLYGA EMKDSILFLN
     PGSTRRPRGG REATYAVIEW DETVRVSFCN IKGELVDSVE MKNLL
//
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