PPBD_BACSU
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 03-AUG-2022, entry version 131.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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};
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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_009966461.1; NZ_CM000487.1.
DR RefSeq; WP_009969242.1; NZ_JNCM01000030.1.
DR PDB; 2YEQ; X-ray; 1.93 A; A/B=57-583.
DR PDBsum; 2YEQ; -.
DR AlphaFoldDB; P42251; -.
DR SMR; P42251; -.
DR STRING; 224308.BSU02620; -.
DR PaxDb; P42251; -.
DR PRIDE; P42251; -.
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 OMA; SCANWEA; -.
DR PhylomeDB; P42251; -.
DR BioCyc; BSUB:BSU02620-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07389; MPP_PhoD; 1.
DR Gene3D; 3.60.21.70; -; 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 Pfam; PF09423; PhoD; 1.
DR Pfam; PF16655; PhoD_N; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
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 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 STRAND 158..161
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 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
