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Database: UniProt
Entry: A0A1I0PN29_9BACT
LinkDB: A0A1I0PN29_9BACT
Original site: A0A1I0PN29_9BACT 
ID   A0A1I0PN29_9BACT        Unreviewed;       248 AA.
AC   A0A1I0PN29;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 5.
DE   RecName: Full=Acid phosphatase {ECO:0000256|PIRNR:PIRNR000897};
DE            EC=3.1.3.2 {ECO:0000256|PIRNR:PIRNR000897};
GN   ORFNames=SAMN04487850_1880 {ECO:0000313|EMBL:SEW15655.1};
OS   Prevotella aff. ruminicola Tc2-24.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=81582 {ECO:0000313|EMBL:SEW15655.1, ECO:0000313|Proteomes:UP000199373};
RN   [1] {ECO:0000313|EMBL:SEW15655.1, ECO:0000313|Proteomes:UP000199373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC2-24 {ECO:0000313|EMBL:SEW15655.1,
RC   ECO:0000313|Proteomes:UP000199373};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR000897};
CC   -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase
CC       family. {ECO:0000256|PIRNR:PIRNR000897}.
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DR   EMBL; FOIQ01000004; SEW15655.1; -; Genomic_DNA.
DR   BioCyc; GCF_900110895:BMY63_RS09080-MONOMER; -.
DR   Proteomes; UP000199373; 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   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   PIRSF; PIRSF000897; Acid_Ptase_ClsA; 1.
DR   PRINTS; PR00483; BACPHPHTASE.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
DR   PROSITE; PS01157; ACID_PHOSPH_CL_A; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000199373};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199373};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    248       Acid phosphatase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5011469312.
FT   DOMAIN      113    224       acidPPc. {ECO:0000259|SMART:SM00014}.
SQ   SEQUENCE   248 AA;  28062 MW;  8E43B7353D4A62C4 CRC64;
     MKQKPLWMLI VILLFCGMTA QAQSADKQES KPYLSVRQLP DLLKWLPAPP DTTSEAFVHD
     IMRYMWGKTQ RLDSVRAAIA IRDAVWDIDS TLAAYYVPFG MEITKEKTPE IYTLMERSIK
     TCDQIGGKAK WFYRRKRPFQ RMHEHMLTRH EEPGLVHNGS YPSGHTIRGW SAALLLSEIN
     PAAADTILAR GMMYGDSRVI VGAHWQSDID AGRLAAGAAC AALHTSREFL DQLAKARAEF
     LRLTAKKD
//
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