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P0AFJ5

- PHOB_ECOLI

UniProt

P0AFJ5 - PHOB_ECOLI

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Protein

Phosphate regulon transcriptional regulatory protein PhoB

Gene

phoB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.

GO - Molecular functioni

  1. bacterial-type RNA polymerase holo enzyme binding Source: EcoCyc
  2. DNA binding Source: UniProtKB-KW
  3. identical protein binding Source: IntAct
  4. phosphorelay response regulator activity Source: InterPro

GO - Biological processi

  1. phosphate ion transport Source: UniProtKB-KW
  2. regulation of DNA-templated transcription, initiation Source: EcoCyc
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Phosphate transport, Transcription, Transcription regulation, Transport, Two-component regulatory system

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PHOB-MONOMER.
ECOL316407:JW0389-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphate regulon transcriptional regulatory protein PhoB
Gene namesi
Name:phoB
Ordered Locus Names:b0399, JW0389
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10728. phoB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229Phosphate regulon transcriptional regulatory protein PhoBPRO_0000081186Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 5314-aspartylphosphate1 PublicationPROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated by PhoR or CreC.1 Publication

Keywords - PTMi

Phosphoprotein

Expressioni

Gene expression databases

GenevestigatoriP0AFJ5.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-1116564,EBI-1116564

Protein-protein interaction databases

DIPiDIP-35852N.
IntActiP0AFJ5. 24 interactions.
MINTiMINT-1313174.
STRINGi511145.b0399.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi12 – 2413Combined sources
Beta strandi28 – 325Combined sources
Helixi35 – 395Combined sources
Beta strandi43 – 453Combined sources
Beta strandi48 – 569Combined sources
Helixi61 – 699Combined sources
Turni72 – 765Combined sources
Beta strandi79 – 846Combined sources
Helixi87 – 926Combined sources
Beta strandi100 – 1067Combined sources
Helixi109 – 12113Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi137 – 1404Combined sources
Turni141 – 1444Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi151 – 1533Combined sources
Helixi157 – 16812Combined sources
Beta strandi171 – 1744Combined sources
Helixi176 – 1838Combined sources
Beta strandi186 – 1883Combined sources
Helixi193 – 20614Combined sources
Helixi207 – 2093Combined sources
Helixi211 – 2144Combined sources
Beta strandi215 – 2184Combined sources
Turni219 – 2213Combined sources
Beta strandi222 – 2254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B00X-ray1.88A/B1-127[»]
1GXPX-ray2.50A/B/E/F124-229[»]
1GXQX-ray2.00A124-229[»]
1QQINMR-A126-229[»]
1ZESX-ray1.90A/B/C1-125[»]
2IYNX-ray2.08A/B/C1-127[»]
2JB9X-ray1.70A/B1-127[»]
2JBAX-ray1.45A/B1-127[»]
2Z33NMR-A126-229[»]
3T72X-ray4.331/4/5/8/9/A/B/E/F/I/J/M/N/R/S/V/W/Z/c/d/g/h/k/l128-229[»]
ProteinModelPortaliP0AFJ5.
SMRiP0AFJ5. Positions 2-123, 125-229.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFJ5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 120120Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0745.
HOGENOMiHOG000034819.
InParanoidiP0AFJ5.
KOiK07657.
OMAiSHPERAY.
OrthoDBiEOG6G4VQG.
PhylomeDBiP0AFJ5.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR001867. Sig_transdc_resp-reg_C.
IPR011879. Sig_transdc_resp-reg_PhoB.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
PF00486. Trans_reg_C. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
SM00862. Trans_reg_C. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
TIGRFAMsiTIGR02154. PhoB. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AFJ5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARRILVVED EAPIREMVCF VLEQNGFQPV EAEDYDSAVN QLNEPWPDLI
60 70 80 90 100
LLDWMLPGGS GIQFIKHLKR ESMTRDIPVV MLTARGEEED RVRGLETGAD
110 120 130 140 150
DYITKPFSPK ELVARIKAVM RRISPMAVEE VIEMQGLSLD PTSHRVMAGE
160 170 180 190 200
EPLEMGPTEF KLLHFFMTHP ERVYSREQLL NHVWGTNVYV EDRTVDVHIR
210 220
RLRKALEPGG HDRMVQTVRG TGYRFSTRF
Length:229
Mass (Da):26,433
Last modified:August 1, 1988 - v1
Checksum:iEB46BA282F1F2C23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04026 Genomic DNA. Translation: CAA27659.1.
U73857 Genomic DNA. Translation: AAB18123.1.
U00096 Genomic DNA. Translation: AAC73502.1.
AP009048 Genomic DNA. Translation: BAE76179.1.
PIRiA24256. RGECFB.
RefSeqiNP_414933.1. NC_000913.3.
YP_488691.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73502; AAC73502; b0399.
BAE76179; BAE76179; BAE76179.
GeneIDi12930822.
945046.
KEGGiecj:Y75_p0387.
eco:b0399.
PATRICi32115943. VBIEscCol129921_0413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04026 Genomic DNA. Translation: CAA27659.1 .
U73857 Genomic DNA. Translation: AAB18123.1 .
U00096 Genomic DNA. Translation: AAC73502.1 .
AP009048 Genomic DNA. Translation: BAE76179.1 .
PIRi A24256. RGECFB.
RefSeqi NP_414933.1. NC_000913.3.
YP_488691.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B00 X-ray 1.88 A/B 1-127 [» ]
1GXP X-ray 2.50 A/B/E/F 124-229 [» ]
1GXQ X-ray 2.00 A 124-229 [» ]
1QQI NMR - A 126-229 [» ]
1ZES X-ray 1.90 A/B/C 1-125 [» ]
2IYN X-ray 2.08 A/B/C 1-127 [» ]
2JB9 X-ray 1.70 A/B 1-127 [» ]
2JBA X-ray 1.45 A/B 1-127 [» ]
2Z33 NMR - A 126-229 [» ]
3T72 X-ray 4.33 1/4/5/8/9/A/B/E/F/I/J/M/N/R/S/V/W/Z/c/d/g/h/k/l 128-229 [» ]
ProteinModelPortali P0AFJ5.
SMRi P0AFJ5. Positions 2-123, 125-229.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35852N.
IntActi P0AFJ5. 24 interactions.
MINTi MINT-1313174.
STRINGi 511145.b0399.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73502 ; AAC73502 ; b0399 .
BAE76179 ; BAE76179 ; BAE76179 .
GeneIDi 12930822.
945046.
KEGGi ecj:Y75_p0387.
eco:b0399.
PATRICi 32115943. VBIEscCol129921_0413.

Organism-specific databases

EchoBASEi EB0721.
EcoGenei EG10728. phoB.

Phylogenomic databases

eggNOGi COG0745.
HOGENOMi HOG000034819.
InParanoidi P0AFJ5.
KOi K07657.
OMAi SHPERAY.
OrthoDBi EOG6G4VQG.
PhylomeDBi P0AFJ5.

Enzyme and pathway databases

BioCyci EcoCyc:PHOB-MONOMER.
ECOL316407:JW0389-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AFJ5.
PROi P0AFJ5.

Gene expression databases

Genevestigatori P0AFJ5.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR011006. CheY-like_superfamily.
IPR001867. Sig_transdc_resp-reg_C.
IPR011879. Sig_transdc_resp-reg_PhoB.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00072. Response_reg. 1 hit.
PF00486. Trans_reg_C. 1 hit.
[Graphical view ]
SMARTi SM00448. REC. 1 hit.
SM00862. Trans_reg_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52172. SSF52172. 1 hit.
TIGRFAMsi TIGR02154. PhoB. 1 hit.
PROSITEi PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12."
    Makino K., Shinagawa H., Amemura M., Nakata A.
    J. Mol. Biol. 190:37-44(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Three-dimensional crystal structure of the transcription factor PhoB receiver domain."
    Sola M., Gomis-Rueth F.-X., Serrano L., Gonzalez A., Coll M.
    J. Mol. Biol. 285:675-687(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-126, PHOSPHORYLATION AT ASP-53.
  6. "Structural comparison of the PhoB and OmpR DNA-binding/transactivation domains and the arrangement of PhoB molecules on the phosphate box."
    Okamura H., Hanaoka S., Nagadoi A., Makino K., Nishimura Y.
    J. Mol. Biol. 295:1225-1236(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 126-229.

Entry informationi

Entry nameiPHOB_ECOLI
AccessioniPrimary (citable) accession number: P0AFJ5
Secondary accession number(s): P08402, Q2MC27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 26, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3