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Database: UniProt
Entry: W4PEB5_9BACE
LinkDB: W4PEB5_9BACE
Original site: W4PEB5_9BACE 
ID   W4PEB5_9BACE            Unreviewed;       187 AA.
AC   W4PEB5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=acid phosphatase {ECO:0000256|ARBA:ARBA00012646};
DE            EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646};
GN   ORFNames=JCM6294_263 {ECO:0000313|EMBL:GAE17504.1};
OS   Bacteroides pyogenes DSM 20611 = JCM 6294.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1121100 {ECO:0000313|EMBL:GAE17504.1, ECO:0000313|Proteomes:UP000018842};
RN   [1] {ECO:0000313|Proteomes:UP000018842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 6294 {ECO:0000313|Proteomes:UP000018842};
RA   Sakamoto M., Oshima K., Suda W., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Strains of Bacteroides pyogenes Isolated
RT   from a Cat and Swine.";
RL   Genome Announc.2:e01242-13(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000032};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00009017}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE17504.1}.
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DR   EMBL; BAIR01000002; GAE17504.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4PEB5; -.
DR   STRING; 1121100.GCA_000428105_00191; -.
DR   eggNOG; COG0671; Bacteria.
DR   Proteomes; UP000018842; Unassembled WGS sequence.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd03397; PAP2_acid_phosphatase; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR001011; Acid_Pase_classA_bac.
DR   InterPro; IPR018296; Acid_Pase_classA_bac_CS.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Pfam; PF01569; PAP2; 1.
DR   PRINTS; PR00483; BACPHPHTASE.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR   PROSITE; PS01157; ACID_PHOSPH_CL_A; 1.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          44..156
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   187 AA;  20786 MW;  9E05D669180BEAF0 CRC64;
     MLRDTPRGDQ AVRDARVGGN GVPMAFSEAF GIEISKEKTP EIHKLVINMR EDAGDLATRH
     AKEHYMRVRP FSFFKENTCN PEQQQELSTN GSYPSGHTAI GWATALVLAE INPARQNEIL
     ERGYEMGQSR VICGYHFQSD VDAARLVASA VVARLHANEA FMKQLEKAKK EFAQLEKAGA
     VKPSENN
//
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