PPB3_BACSU
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 03-AUG-2022, entry version 150.
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; Firmicutes; 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; P19405; -.
DR PRIDE; P19405; -.
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 OMA; NIYAYAN; -.
DR PhylomeDB; P19405; -.
DR BioCyc; BSUB:BSU05740-MON; -.
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; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 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
