APHA_SALTM
ID APHA_SALTM Reviewed; 237 AA.
AC Q540U1; Q5MB24;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Class B acid phosphatase {ECO:0000312|EMBL:AAM95781.1};
DE Short=CBAP;
DE EC=3.1.3.2 {ECO:0000269|PubMed:14501135, ECO:0000312|EMBL:AAW22868.1};
DE Flags: Precursor;
GN Name=aphA {ECO:0000312|EMBL:AAM95781.1};
OS Salmonella typhimurium.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90371;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM95781.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-38 AND 40-46,
RP FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR
RP LOCATION, AND CRYSTALLIZATION.
RC STRAIN=MD6001 {ECO:0000312|EMBL:AAW22868.1};
RX PubMed=14501135; DOI=10.1107/s0907444903018006;
RA Makde R.D., Kumar V., Gupta G.D., Jasti J., Singh T.P., Mahajan S.K.;
RT "Expression, purification, crystallization and preliminary X-ray
RT diffraction studies of recombinant class B non-specific acid phosphatase of
RT Salmonella typhimurium.";
RL Acta Crystallogr. D 59:1849-1852(2003).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-237 OF WILD-TYPE AND MUTANTS
RP ARG/ASN-177 IN COMPLEXES WITH CAMP; PHOSPHATE AND MAGNESIUM IONS, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP ACTIVE SITE, AND MUTAGENESIS OF LYS-177 AND ASP-196.
RC STRAIN=MD6001;
RX PubMed=17570338; DOI=10.1016/j.abb.2007.03.043;
RA Makde R.D., Gupta G.D., Mahajan S.K., Kumar V.;
RT "Structural and mutational analyses reveal the functional role of active-
RT site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein.";
RL Arch. Biochem. Biophys. 464:70-79(2007).
CC -!- FUNCTION: Dephosphorylates several organic phosphate monoesters
CC (PubMed:14501135, PubMed:17570338). Also has a phosphotransferase
CC activity catalyzing the transfer of low-energy phosphate groups from
CC organic phosphate monoesters to free hydroxyl groups of various organic
CC compounds (By similarity). {ECO:0000250|UniProtKB:P58683,
CC ECO:0000269|PubMed:14501135, ECO:0000269|PubMed:17570338}.
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:0000269|PubMed:14501135, ECO:0000269|PubMed:17570338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17570338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17570338};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for pNPP (in the presence of 1 mM MgCl(2) at 37 degrees
CC Celsius and pH 5.6) {ECO:0000269|PubMed:17570338};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14501135,
CC ECO:0000269|PubMed:17570338}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:14501135}.
CC -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase family.
CC {ECO:0000250|UniProtKB:P0AE22}.
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DR EMBL; AY125468; AAM95781.1; -; Genomic_DNA.
DR EMBL; AY841758; AAW22868.1; -; Genomic_DNA.
DR RefSeq; WP_000724435.1; NZ_WXYU01000001.1.
DR PDB; 1Z5G; X-ray; 2.00 A; A/B/C/D=24-237.
DR PDB; 1Z5U; X-ray; 2.30 A; A/B/C/D=24-237.
DR PDB; 1Z88; X-ray; 2.10 A; A/B/C/D=24-237.
DR PDB; 2AUT; X-ray; 2.25 A; A/B/C/D=24-237.
DR PDBsum; 1Z5G; -.
DR PDBsum; 1Z5U; -.
DR PDBsum; 1Z88; -.
DR PDBsum; 2AUT; -.
DR AlphaFoldDB; Q540U1; -.
DR SMR; Q540U1; -.
DR eggNOG; COG3700; Bacteria.
DR OMA; PEFWEKM; -.
DR SABIO-RK; Q540U1; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Magnesium;
KW Metal-binding; Periplasm; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:14501135"
FT CHAIN 24..237
FT /note="Class B acid phosphatase"
FT /evidence="ECO:0000269|PubMed:14501135"
FT /id="PRO_0000414922"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17570338"
FT ACT_SITE 71
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:17570338"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17570338"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17570338"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17570338"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17570338"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17570338"
FT MUTAGEN 177
FT /note="K->N: 40-fold reduction in phosphatase activity.
FT 5.6-fold increase in KM for pNPP in presence of 1 mM
FT MgCl(2)."
FT /evidence="ECO:0000269|PubMed:17570338"
FT MUTAGEN 177
FT /note="K->R: 20-fold reduction in phosphatase activity.
FT Nearly 2-fold increase in KM for pNPP in presence of 1 mM
FT MgCl(2)."
FT /evidence="ECO:0000269|PubMed:17570338"
FT MUTAGEN 196
FT /note="D->N: 6-fold reduction in phosphatase activity.
FT 10000-fold decrease in affinity for Mg(2+). 18-fold
FT increase in KM for pNPP in presence of 1 mM MgCl(2). KM is
FT 0.79 mM for pNPP in the presence of 10 mM MgCl(2)."
FT /evidence="ECO:0000269|PubMed:17570338"
FT CONFLICT 118
FT /note="V -> A (in Ref. 1; AAW22868)"
FT /evidence="ECO:0000305"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:1Z5G"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:1Z5G"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1Z5G"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1Z5G"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:1Z5G"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:1Z5G"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1Z5G"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:1Z5G"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:1Z5G"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:1Z5G"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1Z5G"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1Z5G"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1Z5G"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:1Z5G"
SQ SEQUENCE 237 AA; 26315 MW; 386E11DC84C16269 CRC64;
MKKITLALSA VCLLFTLNHS ANALVSSPST LNPGTNVAKL AEQAPVHWVS VAQIENSLTG
RPPMAVGFDI DDTVLFSSPG FWRGKKTYSP DSDDYLKNPA FWEKMNNGWD EFSIPKEVAR
QLIDMHVRRG DSIYFVTGRS QTKTETVSKT LADNFHIPAA NMNPVIFAGD KPEQNTKVQW
LQEKNMRIFY GDSDNDITAA RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY
