Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19405

- PPB3_BACSU

UniProt

P19405 - PPB3_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Alkaline phosphatase 3

Gene

phoB

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

Protein has several cofactor binding sites:
  • Mg2+Note: Binds 1 Mg(2+) ion.
  • Zn2+Note: Binds 2 Zn(2+) 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

  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: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: 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.BSU05740.

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.
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.

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 .
PIRi C69676.
RefSeqi NP_388455.2. NC_000964.3.

3D structure databases

ProteinModelPortali P19405.
SMRi P19405. Positions 45-454.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU05740.

Proteomic databases

PaxDbi P19405.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12393 ; CAB12393 ; BSU05740 .
GeneIDi 938004.
KEGGi bsu:BSU05740.
PATRICi 18972762. VBIBacSub10457_0602.

Organism-specific databases

GenoListi BSU05740. [Micado ]

Phylogenomic databases

eggNOGi COG1785.
HOGENOMi HOG000099116.
InParanoidi P19405.
KOi K01077.
OrthoDBi EOG661H4G.
PhylomeDBi P19405.

Enzyme and pathway databases

BioCyci BSUB:BSU05740-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. "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: November 26, 2014
This is version 115 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