ID J2WN71_9SPHN Unreviewed; 284 AA.
AC J2WN71;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=acid phosphatase {ECO:0000256|ARBA:ARBA00012646};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646};
GN ORFNames=PMI04_01791 {ECO:0000313|EMBL:EJK83675.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK83675.1, ECO:0000313|Proteomes:UP000006480};
RN [1] {ECO:0000313|EMBL:EJK83675.1, ECO:0000313|Proteomes:UP000006480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK83675.1,
RC ECO:0000313|Proteomes:UP000006480};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJK83675.1}.
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DR EMBL; AJVL01000042; EJK83675.1; -; Genomic_DNA.
DR AlphaFoldDB; J2WN71; -.
DR STRING; 1144307.PMI04_01791; -.
DR PATRIC; fig|1144307.3.peg.1740; -.
DR eggNOG; COG0671; Bacteria.
DR Proteomes; UP000006480; 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 155..264
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 30378 MW; 5C8D338A02A071B8 CRC64;
MLNIGSERPE NGEHSDMRMT RRQGSARLAM LSSVLLLTGC ATAPAPTSLS TTPVPPTSIE
AVGLLSKTFP LPKGYLDPKS LPDSLALLPP PPAEGTAAKA ADQEAFRDGK AAPADRQALA
ASDADLGWPH VVSSFEQIVG VSLSDGSKPH TEMLLRRSMT DAALATYRAK NHYQRVRPFV
ENKSDTCRPQ DEAMLRTDGS YPSGHTAIGW ILALTLTDLA PDKTDALLQR GYAFGQSRVV
CRAHWLSDTT AGRVIASAAY ARLQSDPTYQ AQLALARAEM AKAP
//