ID G8UNG8_TANFA Unreviewed; 259 AA.
AC G8UNG8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Acid phosphatase {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000897};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000897};
GN OrderedLocusNames=BFO_0781 {ECO:0000313|EMBL:AEW20507.1};
OS Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS 5666 / FDC 338) (Bacteroides forsythus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW20507.1, ECO:0000313|Proteomes:UP000005436};
RN [1] {ECO:0000313|Proteomes:UP000005436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC {ECO:0000313|Proteomes:UP000005436};
RA Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA Shetty J., Torralba M., Gill S., Nelson K.;
RT "Complete sequence of Tannerella forsythia ATCC 43037.";
RL Submitted (DEC-2011) 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|ARBA:ARBA00000032,
CC ECO:0000256|PIRNR:PIRNR000897};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009017, ECO:0000256|PIRNR:PIRNR000897}.
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DR EMBL; CP003191; AEW20507.1; -; Genomic_DNA.
DR RefSeq; WP_014224216.1; NC_016610.1.
DR AlphaFoldDB; G8UNG8; -.
DR STRING; 203275.BFO_0781; -.
DR GeneID; 34758101; -.
DR KEGG; tfo:BFO_0781; -.
DR PATRIC; fig|203275.8.peg.697; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_079861_0_0_10; -.
DR Proteomes; UP000005436; Chromosome.
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 PIRSF; PIRSF000897; Acid_Ptase_ClsA; 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 Hydrolase {ECO:0000256|PIRNR:PIRNR000897, ECO:0000313|EMBL:AEW20507.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000005436};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 114..226
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 259 AA; 28972 MW; 842CCD3D03528768 CRC64;
MKKKTFIAVV LSIISVAVFG QEKIKDVRTN PTLYFLQIED VARSLDLLAP PPQPGSILFL
HDQAQYQWGK MQRNTPRGEQ AFSDANVDGD GVPQAFSEAF GVRISKETTP EIHKLVLNMR
EDAGDLATRG AKEHYMRMRP FAFYQEETCN PKQQQELSTN GSYPSGHTAI GWATALVLAE
INVDRQNEIL KRGYEMGQSR VICGYHFQSD VDAARLVASA VVARLHANEN FMVQLGKAKQ
EFAKLVKEGK VKKSETQVN
//
