ID A0A0S8K1W6_9BACE Unreviewed; 257 AA.
AC A0A0S8K1W6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Acid phosphatase {ECO:0000256|PIRNR:PIRNR000897};
DE EC=3.1.3.2 {ECO:0000256|PIRNR:PIRNR000897};
GN ORFNames=AMS26_06335 {ECO:0000313|EMBL:KPL15977.1};
OS Bacteroides sp. SM23_62.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL15977.1, ECO:0000313|Proteomes:UP000050819};
RN [1] {ECO:0000313|EMBL:KPL15977.1, ECO:0000313|Proteomes:UP000050819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62 {ECO:0000313|EMBL:KPL15977.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL15977.1}.
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DR EMBL; LJUP01000040; KPL15977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8K1W6; -.
DR PATRIC; fig|1703352.3.peg.2430; -.
DR Proteomes; UP000050819; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000897}.
FT DOMAIN 116..230
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 257 AA; 28306 MW; 1E5993162096EA67 CRC64;
MKFILIALTS AILVTGCGTK SITSLSKEIR EIGPGILEGY LPARELPNSL FLVPPPPQEG
STAFQLDQEI AAKYIASDDE TRKQQAARDA VLAFPEALHA FNIVLDRPVS KDTTPHLYMI
LRRTVADAGL STYMAKNHYQ RARPFMVNNT PTCSPESEKH LREDGSYPSG HAAIGWAWAL
ILAEVFPEQA NVILKRGEEF GISRSVCNVH WHSDVLAGRM MGAAVVARLH ANADFMIDLE
AAKKEINKLK KQLKQGS
//