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P19406

- PPB4_BACSU

UniProt

P19406 - PPB4_BACSU

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Protein

Alkaline phosphatase 4

Gene

phoA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

Binds 1 magnesium ion.
Binds 2 zinc ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi58 – 581MagnesiumBy similarity
Metal bindingi58 – 581Zinc 2By similarity
Active sitei108 – 1081Phosphoserine intermediatePROSITE-ProRule annotation
Metal bindingi161 – 1611MagnesiumBy similarity
Metal bindingi282 – 2821MagnesiumBy similarity
Metal bindingi287 – 2871Zinc 1By similarity
Metal bindingi291 – 2911Zinc 1By similarity
Metal bindingi329 – 3291Zinc 2By similarity
Metal bindingi330 – 3301Zinc 2By similarity
Metal bindingi423 – 4231Zinc 1By similarity

GO - Molecular functioni

  1. alkaline phosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU09410-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline phosphatase 4 (EC:3.1.3.1)
Alternative name(s):
Alkaline phosphatase IV
Short name:
APase IV
Gene namesi
Name:phoA
Synonyms:phoAIV
Ordered Locus Names:BSU09410
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU09410. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 41411 PublicationAdd
BLAST
Chaini42 – 461420Alkaline phosphatase 4PRO_0000024011Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP19406.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi224308.BSU09410.

Structurei

3D structure databases

ProteinModelPortaliP19406.
SMRiP19406. Positions 51-458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alkaline phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1785.
HOGENOMiHOG000099116.
InParanoidiP19406.
KOiK01077.
OrthoDBiEOG661H4G.
PhylomeDBiP19406.

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.

P19406-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKMSLFQNM KSKLLPIAAV SVLTAGIFAG AELQQTEKAS AKKQDKAEIR
60 70 80 90 100
NVIVMIGDGM GTPYIRAYRS MKNNGDTPNN PKLTEFDRNL TGMMMTHPDD
110 120 130 140 150
PDYNITDSAA AGTALATGVK TYNNAIGVDK NGKKVKSVLE EAKQQGKSTG
160 170 180 190 200
LVATSEINHA TPAAYGAHNE SRKNMDQIAN SYMDDKIKGK HKIDVLLGGG
210 220 230 240 250
KSYFNRKDRN LTKEFKQAGY SYVTTKQALK KNKDQQVLGL FADGGLAKAL
260 270 280 290 300
DRDSKTPSLK DMTVSAIDRL NQNKKGFFLM VEGSQIDWAA HDNDTVGAMS
310 320 330 340 350
EVKDFEQAYK AAIEFAKKDK HTLVIATADH TTGGFTIGAN GEKNWHAEPI
360 370 380 390 400
LSAKKTPEFM AKKISEGKPV KDVLARYANL KVTSEEIKSV EAAAQADKSK
410 420 430 440 450
GASKAIIKIF NTRSNSGWTS TDHTGEEVPV YAYGPGKEKF RGLINNTDQA
460
NIIFKILKTG K
Length:461
Mass (Da):50,274
Last modified:June 16, 2009 - v4
Checksum:iA2AD9309026889FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501R → K AA sequence (PubMed:2105301)Curated
Sequence conflicti208 – 2081D → N in AAA18323. (PubMed:8113174)Curated
Sequence conflicti208 – 2081D → N in CAA74486. (PubMed:9579061)Curated
Sequence conflicti208 – 2081D → N(PubMed:1898729)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U02550 Unassigned DNA. Translation: AAA18323.1.
Y14082 Genomic DNA. Translation: CAA74486.1.
AL009126 Genomic DNA. Translation: CAB12780.2.
L26337 Genomic DNA. Translation: AAA22812.1.
PIRiB69676.
RefSeqiNP_388822.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12780; CAB12780; BSU09410.
GeneIDi936265.
KEGGibsu:BSU09410.
PATRICi18973578. VBIBacSub10457_0983.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U02550 Unassigned DNA. Translation: AAA18323.1 .
Y14082 Genomic DNA. Translation: CAA74486.1 .
AL009126 Genomic DNA. Translation: CAB12780.2 .
L26337 Genomic DNA. Translation: AAA22812.1 .
PIRi B69676.
RefSeqi NP_388822.2. NC_000964.3.

3D structure databases

ProteinModelPortali P19406.
SMRi P19406. Positions 51-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU09410.

Proteomic databases

PaxDbi P19406.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12780 ; CAB12780 ; BSU09410 .
GeneIDi 936265.
KEGGi bsu:BSU09410.
PATRICi 18973578. VBIBacSub10457_0983.

Organism-specific databases

GenoListi BSU09410. [Micado ]

Phylogenomic databases

eggNOGi COG1785.
HOGENOMi HOG000099116.
InParanoidi P19406.
KOi K01077.
OrthoDBi EOG661H4G.
PhylomeDBi P19406.

Enzyme and pathway databases

BioCyci BSUB:BSU09410-MONOMER.

Family and domain databases

Gene3Di 3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view ]
Pfami PF00245. Alk_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR00113. ALKPHPHTASE.
SMARTi SM00098. alkPPc. 1 hit.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPPB4_BACSU
AccessioniPrimary (citable) accession number: P19406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: June 16, 2009
Last modified: October 29, 2014
This is version 118 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