PPB4_BACSU
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 03-AUG-2022, entry version 155.
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; Firmicutes; 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 / NCIMB
RC 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; P19406; -.
DR PRIDE; P19406; -.
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 OMA; NLTGMMM; -.
DR PhylomeDB; P19406; -.
DR BioCyc; BSUB:BSU09410-MON; -.
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; 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..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
