ID APHA_HAEIN Reviewed; 236 AA. AC P44009; P44730; P77869; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-SEP-2023, entry version 120. DE RecName: Full=Class B acid phosphatase; DE Short=CBAP; DE EC=3.1.3.2 {ECO:0000250|UniProtKB:Q540U1}; DE Flags: Precursor; GN Name=aphA; Synonyms=napA; OrderedLocusNames=HI_0494/HI_0495; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CCUG 7317/A; RA Rossolini G.M., Bonci A., Schippa S., Iori P., Thaller M.C.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C., RA Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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). {ECO:0000250}. 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:Q540U1}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q540U1}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q540U1}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22151.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305}; CC Sequence=AAC22152.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305}; 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; L42023; AAC22151.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC22152.1; ALT_FRAME; Genomic_DNA. DR EMBL; Y07615; CAA68889.1; -; Genomic_DNA. DR PIR; T09434; T09434. DR RefSeq; NP_438653.1; NC_000907.1. DR AlphaFoldDB; P44009; -. DR SMR; P44009; -. DR STRING; 71421.HI_0494; -. DR EnsemblBacteria; AAC22151; AAC22151; HI_0494. DR EnsemblBacteria; AAC22152; AAC22152; HI_0495. DR KEGG; hin:HI_0494; -. DR KEGG; hin:HI_0495; -. DR PATRIC; fig|71421.8.peg.512; -. DR eggNOG; COG3700; Bacteria. DR HOGENOM; CLU_081496_0_0_6; -. DR OrthoDB; 2234478at2; -. DR PhylomeDB; P44009; -. DR Proteomes; UP000000579; 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 CDD; cd07499; HAD_CBAP; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01672; AphA; 1. DR Pfam; PF03767; Acid_phosphat_B; 1. DR PIRSF; PIRSF017818; Acid_Ptase_B; 1. DR SFLD; SFLDG01127; C1.3:_Acid_Phosphatase_Like; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 1: Evidence at protein level; KW Hydrolase; Magnesium; Metal-binding; Periplasm; Reference proteome; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..236 FT /note="Class B acid phosphatase" FT /id="PRO_0000024005" FT ACT_SITE 67 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q540U1" FT ACT_SITE 69 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q540U1" FT BINDING 67 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q540U1" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q540U1" FT BINDING 136..137 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q540U1" FT BINDING 176 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q540U1" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q540U1" FT CONFLICT 73 FT /note="Missing (in Ref. 2; CAA68889)" FT /evidence="ECO:0000305" SQ SEQUENCE 236 AA; 26271 MW; D5D7091AC6BB4418 CRC64; MKNVMKLSVI ALLTAAAVPA MAGKTEPYTQ SGTNAREMLQ EQAIHWISVD QIKQSLEGKA PINVSFDIDD TVMLFSSPCF YHGQQKFSPG KHDYLKNQDF WNEVNAGCDK YSIPKQIAID LINMHQARGD QVYFFTGRTA GKVDGVTPIL EKTFNIKNMH PVEFMGSRER TTKYNKTPAI ISHKVSIHYG DSDDDVLAAK EAGVRGIRLM RAANSTYQPM PTLGGYGEEV LINSSY //