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P19405 (PPB3_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkaline phosphatase 3
EC=3.1.3.1
Alternative name(s):
Alkaline phosphatase III
Short name=APase III
Gene names
Name:phoB
Synonyms:phoAIII
Ordered Locus Names:BSU05740
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 magnesium ion.

Binds 2 zinc ions.

Subunit structure

Monomer.

Sequence similarities

Belongs to the alkaline phosphatase family.

Ontologies

Keywords
   DomainSignal
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdephosphorylation

Inferred from electronic annotation. Source: GOC

   Molecular_functionalkaline phosphatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.6
Chain33 – 462430Alkaline phosphatase 3
PRO_0000024010

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding521Magnesium By similarity
Metal binding521Zinc 2 By similarity
Metal binding1541Magnesium By similarity
Metal binding2751Magnesium By similarity
Metal binding2801Zinc 1 By similarity
Metal binding2841Zinc 1 By similarity
Metal binding3221Zinc 2 By similarity
Metal binding3231Zinc 2 By similarity
Metal binding4191Zinc 1 By similarity

Experimental info

Sequence conflict2151Y → S Ref.1
Sequence conflict234 – 2352FA → LP Ref.1
Sequence conflict3341G → S in BAA19698. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P19405 [UniParc].

Last modified July 7, 2009. Version 4.
Checksum: CB0F8FB855D17231

FASTA46250,494
        10         20         30         40         50         60 
MKKFPKKLLP IAVLSSIAFS SLASGSVPEA SAQEKKKGNQ DEIKNVIVLI GDGMGVSYTS 

        70         80         90        100        110        120 
AYRYLKDNKK TKVVEPTAFD QYLVGQQTTY PDDPEQNVTD SAAAATAMSA GIKTYNNAIA 

       130        140        150        160        170        180 
VDNDGSEAKT VLEAAKEKGK ATGLVATSEI THATPASFGS HDHSRKNMNS IADDYFDEMV 

       190        200        210        220        230        240 
NGKHKIDVLL GGGKSNFDRK DRNLIKEFKK AGYSYVDDRK DMLKNKDSQV LGLFADGGLP 

       250        260        270        280        290        300 
KKIDRTKDIP SLKDMTNTAI KKLNKDKDGF FLMVEGSQID WAGHDNDIVG AMSEMEDFEQ 

       310        320        330        340        350        360 
AYKAAIDFAK KDKHTLVVAT ADHSTGGYSI GADGIYNWFS EPIKAAKRTP DFMAEKIADG 

       370        380        390        400        410        420 
ADVEKTLKTY IDQKKLALTK AEIQSVEEAA KSKEVLDIDN AIENIFNKRS HTGWTTGGHT 

       430        440        450        460 
GEDVPVYAYG PSSETFAGQI DNTEIAKNVF KALQYNIKIN DK

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D88802 Genomic DNA. Translation: BAA19698.1.
AL009126 Genomic DNA. Translation: CAB12393.2.
M33634 Genomic DNA. Translation: AAA22658.1.
PIRC69676.
RefSeqNP_388455.2. NC_000964.3.

3D structure databases

ProteinModelPortalP19405.
SMRP19405. Positions 45-454.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU05740.

Proteomic databases

PaxDbP19405.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12393; CAB12393; BSU05740.
GeneID938004.
KEGGbsu:BSU05740.
PATRIC18972762. VBIBacSub10457_0602.

Organism-specific databases

GenoListBSU05740. [Micado]

Phylogenomic databases

eggNOGCOG1785.
HOGENOMHOG000099116.
KOK01077.
ProtClustDBCLSK886792.

Enzyme and pathway databases

BioCycBSUB:BSU05740-MONOMER.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00113. ALKPHPHTASE.
SMARTSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMSSF53649. Alkaline_phosphatase_core. 1 hit.
PROSITEPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPB3_BACSU
AccessionPrimary (citable) accession number: P19405
Secondary accession number(s): O05498
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 7, 2009
Last modified: May 1, 2013
This is version 107 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents