APHA_PROMH
ID APHA_PROMH Reviewed; 237 AA.
AC B4ET41;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Class B acid phosphatase {ECO:0000250|UniProtKB:P0AE22, ECO:0000312|EMBL:CAR41704.1};
DE Short=CBAP {ECO:0000250|UniProtKB:P0AE22};
DE EC=3.1.3.2 {ECO:0000250|UniProtKB:P0AE22, ECO:0000312|EMBL:CAR41704.1};
DE Flags: Precursor;
GN Name=aphA {ECO:0000312|EMBL:CAR41704.1}; OrderedLocusNames=PMI0729;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1] {ECO:0000312|EMBL:CAR41704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000269|PubMed:18375554};
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
CC -!- FUNCTION: Dephosphorylates several organic phosphate monoesters. Also
CC has a phosphotransferase activity catalyzing the transfer of low-energy
CC phosphate groups from organic phosphate monoesters to free hydroxyl
CC groups of various organic compounds (By similarity).
CC {ECO:0000250|UniProtKB:P0AE22}.
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:0000250|UniProtKB:P0AE22};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0AE22};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0AE22};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AE22}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0AE22}.
CC -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase family.
CC {ECO:0000250|UniProtKB:P0AE22}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM942759; CAR41704.1; -; Genomic_DNA.
DR RefSeq; WP_004247637.1; NC_010554.1.
DR AlphaFoldDB; B4ET41; -.
DR SMR; B4ET41; -.
DR STRING; 529507.PMI0729; -.
DR EnsemblBacteria; CAR41704; CAR41704; PMI0729.
DR GeneID; 6803528; -.
DR KEGG; pmr:PMI0729; -.
DR eggNOG; COG3700; Bacteria.
DR HOGENOM; CLU_081496_0_0_6; -.
DR OMA; PEFWEKM; -.
DR Proteomes; UP000008319; 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR005519; Acid_phosphat_B-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR010025; HAD-SF_ppase_IIIB_AphA.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF03767; Acid_phosphat_B; 1.
DR PIRSF; PIRSF017818; Acid_Ptase_B; 1.
DR SFLD; SFLDG01127; C1.3:_Acid_Phosphatase_Like; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01672; AphA; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..237
FT /note="Class B acid phosphatase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000415228"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT ACT_SITE 71
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AE22"
SQ SEQUENCE 237 AA; 26418 MW; 330F7E7A4CA0FCE0 CRC64;
MRKVTLTLSA IALALSLNGA AMAKVHMPEV VSPGVTVTEL AHQQPIKWVS VAEIEKSLEG
QAPMAVGFDI DDTVLFSSPG FYRGKLEYSP NDFSYLKNPE FWEKMNNEWD KFSMPKQVGI
DLVQMHLKRG DTVYFITGRT QTKTETVTKY VQEGLNIPAD KMQPVIFAGD QPGANNKVSW
MRDHKLKIYY GDADADIAAA DELNIRGIRI LRAANSSYQP LPKAGQFGEE VVINSEY