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P19406 (PPB4_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 4
EC=3.1.3.1
Alternative name(s):
Alkaline phosphatase IV
Short name=APase IV
Gene names
Name:phoA
Synonyms:phoAIV
Ordered Locus Names:BSU09410
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length461 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 – 4141 Ref.7
Chain42 – 461420Alkaline phosphatase 4
PRO_0000024011

Sites

Active site1081Phosphoserine intermediate By similarity
Metal binding581Magnesium By similarity
Metal binding581Zinc 2 By similarity
Metal binding1611Magnesium By similarity
Metal binding2821Magnesium By similarity
Metal binding2871Zinc 1 By similarity
Metal binding2911Zinc 1 By similarity
Metal binding3291Zinc 2 By similarity
Metal binding3301Zinc 2 By similarity
Metal binding4231Zinc 1 By similarity

Experimental info

Sequence conflict501R → K AA sequence Ref.7
Sequence conflict2081D → N in AAA18323. Ref.1
Sequence conflict2081D → N in CAA74486. Ref.2
Sequence conflict2081D → N Ref.5

Sequences

Sequence LengthMass (Da)Tools
P19406 [UniParc].

Last modified June 16, 2009. Version 4.
Checksum: A2AD9309026889FE

FASTA46150,274
        10         20         30         40         50         60 
MKKMSLFQNM KSKLLPIAAV SVLTAGIFAG AELQQTEKAS AKKQDKAEIR NVIVMIGDGM 

        70         80         90        100        110        120 
GTPYIRAYRS MKNNGDTPNN PKLTEFDRNL TGMMMTHPDD PDYNITDSAA AGTALATGVK 

       130        140        150        160        170        180 
TYNNAIGVDK NGKKVKSVLE EAKQQGKSTG LVATSEINHA TPAAYGAHNE SRKNMDQIAN 

       190        200        210        220        230        240 
SYMDDKIKGK HKIDVLLGGG KSYFNRKDRN LTKEFKQAGY SYVTTKQALK KNKDQQVLGL 

       250        260        270        280        290        300 
FADGGLAKAL DRDSKTPSLK DMTVSAIDRL NQNKKGFFLM VEGSQIDWAA HDNDTVGAMS 

       310        320        330        340        350        360 
EVKDFEQAYK AAIEFAKKDK HTLVIATADH TTGGFTIGAN GEKNWHAEPI LSAKKTPEFM 

       370        380        390        400        410        420 
AKKISEGKPV KDVLARYANL KVTSEEIKSV EAAAQADKSK GASKAIIKIF NTRSNSGWTS 

       430        440        450        460 
TDHTGEEVPV YAYGPGKEKF RGLINNTDQA NIIFKILKTG K

« Hide

References

« Hide 'large scale' references
[1]"Sequential action of two-component genetic switches regulates the PHO regulon in Bacillus subtilis."
Hulett F.M., Lee J., Shi L., Sun G., Chesnut R., Sharkova E., Duggan M.F., Kapp N.
J. Bacteriol. 176:1348-1358(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[2]"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[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 208.
[5]"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] OF 39-461.
Strain: 168 / JH642.
[6]"The Bacillus subtilis phoAIV gene: effects of in vitro inactivation on total alkaline phosphatase production."
Kapp N.V., Edwards C.W., Chesnut R.S., Hulett F.M.
Gene 96:95-100(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-142.
Strain: 168 / JH642.
[7]"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 42-63.
[8]"Cloning and characterization of spoVR, a gene from Bacillus subtilis involved in spore cortex formation."
Beall B.W., Moran C.P. Jr.
J. Bacteriol. 176:2003-2012(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 433-461.
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U02550 Unassigned DNA. Translation: AAA18323.1.
Y14082 Genomic DNA. Translation: CAA74486.1.
AL009126 Genomic DNA. Translation: CAB12780.2.
L26337 Genomic DNA. Translation: AAA22812.1.
PIRB69676.
RefSeqNP_388822.2. NC_000964.3.

3D structure databases

ProteinModelPortalP19406.
SMRP19406. Positions 51-458.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU09410.

Proteomic databases

PaxDbP19406.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12780; CAB12780; BSU09410.
GeneID936265.
KEGGbsu:BSU09410.
PATRIC18973578. VBIBacSub10457_0983.

Organism-specific databases

GenoListBSU09410. [Micado]

Phylogenomic databases

eggNOGCOG1785.
HOGENOMHOG000099116.
KOK01077.
ProtClustDBCLSK2460902.

Enzyme and pathway databases

BioCycBSUB:BSU09410-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 namePPB4_BACSU
AccessionPrimary (citable) accession number: P19406
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: June 16, 2009
Last modified: May 1, 2013
This is version 111 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