APHA_XENBS
ID APHA_XENBS Reviewed; 237 AA.
AC D3UWV6;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Class B acid phosphatase {ECO:0000250|UniProtKB:P0AE22, ECO:0000312|EMBL:CBJ79941.1};
DE Short=CBAP {ECO:0000250|UniProtKB:P0AE22};
DE EC=3.1.3.2 {ECO:0000250|UniProtKB:P0AE22, ECO:0000312|EMBL:CBJ79941.1};
DE Flags: Precursor;
GN Name=aphA {ECO:0000312|EMBL:CBJ79941.1}; OrderedLocusNames=XBJ1_0800;
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818;
RN [1] {ECO:0000312|EMBL:CBJ79941.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004;
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
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}.
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DR EMBL; FN667741; CBJ79941.1; -; Genomic_DNA.
DR RefSeq; WP_012987374.1; NC_013892.1.
DR AlphaFoldDB; D3UWV6; -.
DR SMR; D3UWV6; -.
DR STRING; 406818.XBJ1_0800; -.
DR EnsemblBacteria; CBJ79941; CBJ79941; XBJ1_0800.
DR GeneID; 8830427; -.
DR KEGG; xbo:XBJ1_0800; -.
DR PATRIC; fig|406818.4.peg.721; -.
DR eggNOG; COG3700; Bacteria.
DR HOGENOM; CLU_081496_0_0_6; -.
DR OMA; PEFWEKM; -.
DR Proteomes; UP000002045; 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_0000415230"
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; 26870 MW; 5BA5B902EC8351AF CRC64;
MRKVTLVFSA IAFAFSLNGV VQAKVQMPES VSSGVTTVEL SQRQAVHWVS VEQIEKSLQD
QPPMAIGFDI DDTVLFSSPG FYRGKLKYSP NDNSYLKNPA FWEKMNNEWD EFSMPKQIGI
ELVQMHLKRG DNIYFITGRT KTKTETVTKY LQEDLHIPAD KMNVVIFAGD DPGKNNKISW
MKEHKLKLYY GDADADIAAA HELNIRGIRI LRASNSSYQP LPKAGRFGEE VVIKSEY
