ID   PPB3_BACSU              Reviewed;         462 AA.
AC   P19405; O05498;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 4.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Alkaline phosphatase 3;
DE            EC=3.1.3.1;
DE   AltName: Full=Alkaline phosphatase III;
DE            Short=APase III;
DE   Flags: Precursor;
GN   Name=phoB; Synonyms=phoAIII; OrderedLocusNames=BSU05740;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1898729; DOI=10.1016/s0021-9258(17)35285-7;
RA   Hulett F.M., Kim M.E., Bookstein C., Kapp N.V., Edwards C.W., Wyckoff H.W.;
RT   "Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing,
RT   and comparisons of deduced amino acid sequence with Escherichia coli
RT   alkaline phosphatase three-dimensional structure.";
RL   J. Biol. Chem. 266:1077-1084(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA   Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA   Ogasawara N.;
RT   "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT   Bacillus subtilis chromosome.";
RL   Microbiology 143:1861-1866(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 334.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC   STRAIN=168;
RX   PubMed=2113910; DOI=10.1128/jb.172.7.3730-3737.1990;
RA   Bookstein C., Edwards C.W., Kapp N.V., Hulett F.M.;
RT   "The Bacillus subtilis 168 alkaline phosphatase III gene: impact of a
RT   phoAIII mutation on total alkaline phosphatase synthesis.";
RL   J. Bacteriol. 172:3730-3737(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 33-62.
RX   PubMed=2105301; DOI=10.1128/jb.172.2.735-740.1990;
RA   Hulett F.M., Bookstein C., Jensen K.;
RT   "Evidence for two structural genes for alkaline phosphatase in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 172:735-740(1990).
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=3.1.3.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR   EMBL; D88802; BAA19698.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12393.2; -; Genomic_DNA.
DR   EMBL; M33634; AAA22658.1; -; Genomic_DNA.
DR   PIR; C69676; C69676.
DR   RefSeq; NP_388455.2; NC_000964.3.
DR   RefSeq; WP_003234119.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; P19405; -.
DR   SMR; P19405; -.
DR   STRING; 224308.BSU05740; -.
DR   PaxDb; 224308-BSU05740; -.
DR   EnsemblBacteria; CAB12393; CAB12393; BSU_05740.
DR   GeneID; 938004; -.
DR   KEGG; bsu:BSU05740; -.
DR   PATRIC; fig|224308.43.peg.602; -.
DR   eggNOG; COG1785; Bacteria.
DR   InParanoid; P19405; -.
DR   OrthoDB; 9794455at2; -.
DR   PhylomeDB; P19405; -.
DR   BioCyc; BSUB:BSU05740-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 1.10.60.40; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW   Phosphoprotein; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:2105301"
FT   CHAIN           33..462
FT                   /note="Alkaline phosphatase 3"
FT                   /id="PRO_0000024010"
FT   ACT_SITE        101
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10042"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         322
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        215
FT                   /note="Y -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234..235
FT                   /note="FA -> LP (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="G -> S (in Ref. 2; BAA19698)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  50494 MW;  CB0F8FB855D17231 CRC64;
     MKKFPKKLLP IAVLSSIAFS SLASGSVPEA SAQEKKKGNQ DEIKNVIVLI GDGMGVSYTS
     AYRYLKDNKK TKVVEPTAFD QYLVGQQTTY PDDPEQNVTD SAAAATAMSA GIKTYNNAIA
     VDNDGSEAKT VLEAAKEKGK ATGLVATSEI THATPASFGS HDHSRKNMNS IADDYFDEMV
     NGKHKIDVLL GGGKSNFDRK DRNLIKEFKK AGYSYVDDRK DMLKNKDSQV LGLFADGGLP
     KKIDRTKDIP SLKDMTNTAI KKLNKDKDGF FLMVEGSQID WAGHDNDIVG AMSEMEDFEQ
     AYKAAIDFAK KDKHTLVVAT ADHSTGGYSI GADGIYNWFS EPIKAAKRTP DFMAEKIADG
     ADVEKTLKTY IDQKKLALTK AEIQSVEEAA KSKEVLDIDN AIENIFNKRS HTGWTTGGHT
     GEDVPVYAYG PSSETFAGQI DNTEIAKNVF KALQYNIKIN DK
//