APHA_SHIFL
ID APHA_SHIFL Reviewed; 237 AA.
AC P0AE23; P32697; P76787; Q57085;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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; OrderedLocusNames=SF4149, S3580;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
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DR EMBL; AE005674; AAN45571.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18626.1; -; Genomic_DNA.
DR RefSeq; NP_709864.2; NC_004337.2.
DR RefSeq; WP_001226928.1; NZ_WPGW01000193.1.
DR AlphaFoldDB; P0AE23; -.
DR SMR; P0AE23; -.
DR STRING; 198214.SF4149; -.
DR EnsemblBacteria; AAN45571; AAN45571; SF4149.
DR EnsemblBacteria; AAP18626; AAP18626; S3580.
DR GeneID; 1027006; -.
DR GeneID; 58462006; -.
DR KEGG; sfl:SF4149; -.
DR KEGG; sfx:S3580; -.
DR PATRIC; fig|198214.7.peg.4896; -.
DR HOGENOM; CLU_081496_0_0_6; -.
DR OrthoDB; 1258380at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; -; 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..25
FT /note="Or 23"
FT /evidence="ECO:0000255"
FT CHAIN 26..237
FT /note="Class B acid phosphatase"
FT /id="PRO_0000043379"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT ACT_SITE 71
FT /note="Proton donor"
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 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q540U1"
SQ SEQUENCE 237 AA; 26104 MW; 35C1BFE6DF9E530D CRC64;
MRKITQAISA VCLLFALNSS AVALASSPSP LNPGTNVARL AEQAPIHWVS VAQIENSLAG
RPPMAVGFDI DDTVLFSSPG FWRGKKTFSP ESEDYLKNPV FWEKMNNGWD EFSIPKEVAR
QLIDMHVRRG DAIFFVTGRS PTKTETVSKT LADNFHIPAT NMNPVIFAGD KPGQNTKSQW
LQDKNIRIFY GDSDNDITAA RDVGARGIRI LRASNSTYKP LPQAGAFGEE VIVNSEY
