ID   PPB4_BACSU              Reviewed;         461 AA.
AC   P19406;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 4.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Alkaline phosphatase 4;
DE            EC=3.1.3.1;
DE   AltName: Full=Alkaline phosphatase IV;
DE            Short=APase IV;
DE   Flags: Precursor;
GN   Name=phoA; Synonyms=phoAIV; OrderedLocusNames=BSU09410;
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 / JH642;
RX   PubMed=8113174; DOI=10.1128/jb.176.5.1348-1358.1994;
RA   Hulett F.M., Lee J., Shi L., Sun G., Chesnut R., Sharkova E., Duggan M.F.,
RA   Kapp N.;
RT   "Sequential action of two-component genetic switches regulates the PHO
RT   regulon in Bacillus subtilis.";
RL   J. Bacteriol. 176:1348-1358(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA   Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA   Venema G., Bron S.;
RT   "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT   subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT   many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL   Microbiology 144:859-875(1998).
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 208.
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 39-461.
RC   STRAIN=168 / JH642;
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-142.
RC   STRAIN=168 / JH642;
RX   PubMed=2125017; DOI=10.1016/0378-1119(90)90346-s;
RA   Kapp N.V., Edwards C.W., Chesnut R.S., Hulett F.M.;
RT   "The Bacillus subtilis phoAIV gene: effects of in vitro inactivation on
RT   total alkaline phosphatase production.";
RL   Gene 96:95-100(1990).
RN   [7]
RP   PROTEIN SEQUENCE OF 42-63.
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).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 433-461.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8144469; DOI=10.1128/jb.176.7.2003-2012.1994;
RA   Beall B.W., Moran C.P. Jr.;
RT   "Cloning and characterization of spoVR, a gene from Bacillus subtilis
RT   involved in spore cortex formation.";
RL   J. Bacteriol. 176:2003-2012(1994).
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; U02550; AAA18323.1; -; Unassigned_DNA.
DR   EMBL; Y14082; CAA74486.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12780.2; -; Genomic_DNA.
DR   EMBL; L26337; AAA22812.1; -; Genomic_DNA.
DR   PIR; B69676; B69676.
DR   RefSeq; NP_388822.2; NC_000964.3.
DR   RefSeq; WP_010886458.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P19406; -.
DR   SMR; P19406; -.
DR   STRING; 224308.BSU09410; -.
DR   PaxDb; 224308-BSU09410; -.
DR   EnsemblBacteria; CAB12780; CAB12780; BSU_09410.
DR   GeneID; 936265; -.
DR   KEGG; bsu:BSU09410; -.
DR   PATRIC; fig|224308.43.peg.983; -.
DR   eggNOG; COG1785; Bacteria.
DR   InParanoid; P19406; -.
DR   OrthoDB; 9794455at2; -.
DR   PhylomeDB; P19406; -.
DR   BioCyc; BSUB:BSU09410-MONOMER; -.
DR   BRENDA; 3.1.3.1; 658.
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..41
FT                   /evidence="ECO:0000269|PubMed:2105301"
FT   CHAIN           42..461
FT                   /note="Alkaline phosphatase 4"
FT                   /id="PRO_0000024011"
FT   ACT_SITE        108
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10042"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         423
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        50
FT                   /note="R -> K (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="D -> N (in Ref. 1; AAA18323, 2; CAA74486 and 5)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   461 AA;  50274 MW;  A2AD9309026889FE CRC64;
     MKKMSLFQNM KSKLLPIAAV SVLTAGIFAG AELQQTEKAS AKKQDKAEIR NVIVMIGDGM
     GTPYIRAYRS MKNNGDTPNN PKLTEFDRNL TGMMMTHPDD PDYNITDSAA AGTALATGVK
     TYNNAIGVDK NGKKVKSVLE EAKQQGKSTG LVATSEINHA TPAAYGAHNE SRKNMDQIAN
     SYMDDKIKGK HKIDVLLGGG KSYFNRKDRN LTKEFKQAGY SYVTTKQALK KNKDQQVLGL
     FADGGLAKAL DRDSKTPSLK DMTVSAIDRL NQNKKGFFLM VEGSQIDWAA HDNDTVGAMS
     EVKDFEQAYK AAIEFAKKDK HTLVIATADH TTGGFTIGAN GEKNWHAEPI LSAKKTPEFM
     AKKISEGKPV KDVLARYANL KVTSEEIKSV EAAAQADKSK GASKAIIKIF NTRSNSGWTS
     TDHTGEEVPV YAYGPGKEKF RGLINNTDQA NIIFKILKTG K
//