ID A0A0Q8QA55_9SPHN Unreviewed; 263 AA.
AC A0A0Q8QA55;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Acid phosphatase {ECO:0000256|PIRNR:PIRNR000897};
DE EC=3.1.3.2 {ECO:0000256|PIRNR:PIRNR000897};
GN ORFNames=ASE00_10975 {ECO:0000313|EMBL:KRB82565.1};
OS Sphingomonas sp. Root710.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB82565.1, ECO:0000313|Proteomes:UP000051854};
RN [1] {ECO:0000313|EMBL:KRB82565.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB82565.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB82565.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB82565.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 family.
CC {ECO:0000256|PIRNR:PIRNR000897}.
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:KRB82565.1}.
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DR EMBL; LMIB01000012; KRB82565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8QA55; -.
DR STRING; 1736594.ASE00_10975; -.
DR Proteomes; UP000051854; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000897};
KW Reference proteome {ECO:0000313|Proteomes:UP000051854};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..263
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006353120"
FT DOMAIN 103..219
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 263 AA; 27821 MW; 790571C153773572 CRC64;
MRVRYGMMIA AAALAGAAGG VMAAGADGAG FLPDGYITLI DVVLPAPIPQ EPRGVADREV
FKLTRALKGT ARWDMAVNDA PSDPASLMRD FGCAARISMT PATAPKTAAL LEKASRDASR
QTNELKAFYK KKRPYLLDPG ETCVAQTDEL TASYDYPSGH AAKSWTWGLI LAELVDDRAA
PILARARAYG ESRVVCGVHN MSAIEAGRMV AASTLAVIRT EPAYQDAVVA ARAELAALRK
TGAPPSAQVC SAEEVLVTQP IFR
//
