ID   PPBD_BACSU              Reviewed;         583 AA.
AC   P42251;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=Alkaline phosphatase D;
DE            Short=APaseD;
DE            EC=3.1.3.1;
DE   Flags: Precursor;
GN   Name=phoD; Synonyms=ycbS; OrderedLocusNames=BSU02620;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 57-76.
RC   STRAIN=168 / JH642;
RX   PubMed=8760916; DOI=10.1099/13500872-142-8-2041;
RA   Eder S., Shi L., Jensen K., Yamane K., Hulett F.M.;
RT   "A Bacillus subtilis secreted phosphodiesterase/alkaline phosphatase is the
RT   product of a Pho regulon gene, phoD.";
RL   Microbiology 142:2041-2047(1996).
RN   [2]
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   [3]
RP   SEQUENCE REVISION TO C-TERMINUS.
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-556.
RC   STRAIN=168;
RX   PubMed=7704254; DOI=10.1099/13500872-141-2-269;
RA   Ogawa K., Akagawa E., Nakamura K., Yamane K.;
RT   "Determination of a 21548 bp nucleotide sequence around the 24 degrees
RT   region of the Bacillus subtilis chromosome.";
RL   Microbiology 141:269-275(1995).
RN   [5]
RP   CHARACTERIZATION.
RC   STRAIN=6060-BC6;
RX   PubMed=25878; DOI=10.1128/jb.134.1.100-107.1978;
RA   Yamane K., Maruo B.;
RT   "Purification and characterization of extracellular soluble and membrane-
RT   bound insoluble alkaline phosphatases possessing phosphodiesterase
RT   activities in Bacillus subtilis.";
RL   J. Bacteriol. 134:100-107(1978).
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   -!- INDUCTION: By phosphate starvation.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has been experimentally proven.
CC   -!- SIMILARITY: Belongs to the PhoD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB47803.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA06483.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U49060; AAB47803.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB12056.2; -; Genomic_DNA.
DR   EMBL; D30808; BAA06483.1; ALT_FRAME; Genomic_DNA.
DR   PIR; D69676; D69676.
DR   RefSeq; NP_388144.2; NC_000964.3.
DR   RefSeq; WP_009969242.1; NC_000964.3.
DR   PDB; 2YEQ; X-ray; 1.93 A; A/B=57-583.
DR   AlphaFoldDB; P42251; -.
DR   SMR; P42251; -.
DR   FunCoup; P42251; 402.
DR   STRING; 224308.BSU02620; -.
DR   PaxDb; 224308-BSU02620; -.
DR   EnsemblBacteria; CAB12056; CAB12056; BSU_02620.
DR   GeneID; 938391; -.
DR   KEGG; bsu:BSU02620; -.
DR   PATRIC; fig|224308.179.peg.272; -.
DR   eggNOG; COG3540; Bacteria.
DR   InParanoid; P42251; -.
DR   OrthoDB; 9763616at2; -.
DR   PhylomeDB; P42251; -.
DR   BioCyc; BSUB:BSU02620-MONOMER; -.
DR   EvolutionaryTrace; P42251; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P42251; -.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07389; MPP_PhoD; 1.
DR   Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR018946; PhoD-like_MPP.
DR   InterPro; IPR038607; PhoD-like_sf.
DR   InterPro; IPR032093; PhoD_N.
DR   InterPro; IPR052900; Phospholipid_Metab_Enz.
DR   PANTHER; PTHR43606:SF2; ALKALINE PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_5G03860); 1.
DR   PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   Pfam; PF09423; PhoD; 1.
DR   Pfam; PF16655; PhoD_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PDBsum; 2YEQ; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Reference proteome;
KW   Signal; Stress response.
FT   SIGNAL          1..56
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000269|PubMed:8760916"
FT   CHAIN           57..583
FT                   /note="Alkaline phosphatase D"
FT                   /id="PRO_0000022088"
FT   REGION          339..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         59
FT                   /note="N -> K"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          100..109
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          112..123
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          143..150
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          158..161
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           162..165
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           189..194
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          200..204
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          228..231
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           235..246
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           249..257
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          258..262
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   TURN            267..269
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           284..301
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           306..308
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          319..323
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   TURN            324..326
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          327..331
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          334..337
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           338..341
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           342..344
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          345..348
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           352..355
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           364..376
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          379..385
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          398..400
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           408..410
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           412..424
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          430..434
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          436..448
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          456..462
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          473..475
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           479..485
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          489..494
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          496..504
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          507..516
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          518..521
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          526..533
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   STRAND          540..545
FT                   /evidence="ECO:0007829|PDB:2YEQ"
FT   HELIX           560..576
FT                   /evidence="ECO:0007829|PDB:2YEQ"
SQ   SEQUENCE   583 AA;  65971 MW;  7734224CB2470319 CRC64;
     MAYDSRFDEW VQKLKEESFQ NNTFDRRKFI QGAGKIAGLS LGLTIAQSVG AFEVNAAPNF
     SSYPFTLGVA SGDPLSDSVV LWTRLAPDPL NGGGMPKQAV PVKWEVAKDE HFRKIVRKGT
     EMAKPSLAHS VHVEADGLEP NKVYYYRFKT GHELSPVGKT KTLPAPGANV PQMTFAFASC
     QQYEHGYYTA YKHMAKEKLD LVFHLGDYIY EYGPNEYVSK TGNVRTHNSA EIITLQDYRN
     RHAQYRSDAN LKAAHAAFPW VVTWDDHEVE NNYANKIPEK GQSVEAFVLR RAAAYQAYYE
     HMPLRISSLP NGPDMQLYRH FTYGNLASFN VLDTRQYRDD QANNDGNKPP SDESRNPNRT
     LLGKEQEQWL FNNLGSSTAH WNVLAQQIFF AKWNFGTSAS PIYSMDSWDG YPAQRERVIN
     FIKSKNLNNV VVLTGDVHAS WASNLHVDFE KTSSKIFGAE FVGTSITSGG NGADKRADTD
     QILKENPHIQ FFNDYRGYVR CTVTPHQWKA DYRVMPFVTE PGAAISTRAS FVYQKDQTGL
     RKVSSTTIQG GVKQSDEVEE DRFFSHNKAH EKQMIKKRAK ITN
//