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Protein

Alkaline phosphatase 3

Gene

phoB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+Note: Binds 1 Mg2+ ion.
  • Zn2+Note: Binds 2 Zn2+ ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521MagnesiumBy similarity
Metal bindingi52 – 521Zinc 2By similarity
Active sitei101 – 1011Phosphoserine intermediatePROSITE-ProRule annotation
Metal bindingi154 – 1541MagnesiumBy similarity
Metal bindingi275 – 2751MagnesiumBy similarity
Metal bindingi280 – 2801Zinc 1By similarity
Metal bindingi284 – 2841Zinc 1By similarity
Metal bindingi322 – 3221Zinc 2By similarity
Metal bindingi323 – 3231Zinc 2By similarity
Metal bindingi419 – 4191Zinc 1By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU05740-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline phosphatase 3 (EC:3.1.3.1)
Alternative name(s):
Alkaline phosphatase III
Short name:
APase III
Gene namesi
Name:phoB
Synonyms:phoAIII
Ordered Locus Names:BSU05740
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU05740. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 462430Alkaline phosphatase 3PRO_0000024010Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP19405.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003223.

Structurei

3D structure databases

ProteinModelPortaliP19405.
SMRiP19405. Positions 45-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alkaline phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1785.
HOGENOMiHOG000099116.
InParanoidiP19405.
KOiK01077.
OMAiDDDTYVT.
OrthoDBiEOG661H4G.
PhylomeDBiP19405.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamiPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00113. ALKPHPHTASE.
SMARTiSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19405-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKFPKKLLP IAVLSSIAFS SLASGSVPEA SAQEKKKGNQ DEIKNVIVLI
60 70 80 90 100
GDGMGVSYTS AYRYLKDNKK TKVVEPTAFD QYLVGQQTTY PDDPEQNVTD
110 120 130 140 150
SAAAATAMSA GIKTYNNAIA VDNDGSEAKT VLEAAKEKGK ATGLVATSEI
160 170 180 190 200
THATPASFGS HDHSRKNMNS IADDYFDEMV NGKHKIDVLL GGGKSNFDRK
210 220 230 240 250
DRNLIKEFKK AGYSYVDDRK DMLKNKDSQV LGLFADGGLP KKIDRTKDIP
260 270 280 290 300
SLKDMTNTAI KKLNKDKDGF FLMVEGSQID WAGHDNDIVG AMSEMEDFEQ
310 320 330 340 350
AYKAAIDFAK KDKHTLVVAT ADHSTGGYSI GADGIYNWFS EPIKAAKRTP
360 370 380 390 400
DFMAEKIADG ADVEKTLKTY IDQKKLALTK AEIQSVEEAA KSKEVLDIDN
410 420 430 440 450
AIENIFNKRS HTGWTTGGHT GEDVPVYAYG PSSETFAGQI DNTEIAKNVF
460
KALQYNIKIN DK
Length:462
Mass (Da):50,494
Last modified:July 7, 2009 - v4
Checksum:iCB0F8FB855D17231
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151Y → S (PubMed:1898729).Curated
Sequence conflicti234 – 2352FA → LP (PubMed:1898729).Curated
Sequence conflicti334 – 3341G → S in BAA19698 (PubMed:9202461).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88802 Genomic DNA. Translation: BAA19698.1.
AL009126 Genomic DNA. Translation: CAB12393.2.
M33634 Genomic DNA. Translation: AAA22658.1.
PIRiC69676.
RefSeqiNP_388455.2. NC_000964.3.
WP_003234119.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12393; CAB12393; BSU05740.
GeneIDi938004.
KEGGibsu:BSU05740.
PATRICi18972762. VBIBacSub10457_0602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88802 Genomic DNA. Translation: BAA19698.1.
AL009126 Genomic DNA. Translation: CAB12393.2.
M33634 Genomic DNA. Translation: AAA22658.1.
PIRiC69676.
RefSeqiNP_388455.2. NC_000964.3.
WP_003234119.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP19405.
SMRiP19405. Positions 45-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003223.

Proteomic databases

PaxDbiP19405.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12393; CAB12393; BSU05740.
GeneIDi938004.
KEGGibsu:BSU05740.
PATRICi18972762. VBIBacSub10457_0602.

Organism-specific databases

GenoListiBSU05740. [Micado]

Phylogenomic databases

eggNOGiCOG1785.
HOGENOMiHOG000099116.
InParanoidiP19405.
KOiK01077.
OMAiDDDTYVT.
OrthoDBiEOG661H4G.
PhylomeDBiP19405.

Enzyme and pathway databases

BioCyciBSUB:BSU05740-MONOMER.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamiPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00113. ALKPHPHTASE.
SMARTiSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure."
    Hulett F.M., Kim M.E., Bookstein C., Kapp N.V., Edwards C.W., Wyckoff H.W.
    J. Biol. Chem. 266:1077-1084(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the Bacillus subtilis chromosome."
    Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y., Ogasawara N.
    Microbiology 143:1861-1866(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH642.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 334.
  5. "The Bacillus subtilis 168 alkaline phosphatase III gene: impact of a phoAIII mutation on total alkaline phosphatase synthesis."
    Bookstein C., Edwards C.W., Kapp N.V., Hulett F.M.
    J. Bacteriol. 172:3730-3737(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
    Strain: 168.
  6. "Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis."
    Hulett F.M., Bookstein C., Jensen K.
    J. Bacteriol. 172:735-740(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-62.

Entry informationi

Entry nameiPPB3_BACSU
AccessioniPrimary (citable) accession number: P19405
Secondary accession number(s): O05498
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 7, 2009
Last modified: July 22, 2015
This is version 119 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.