PHOB_ECOLI
ID PHOB_ECOLI Reviewed; 229 AA.
AC P0AFJ5; P08402; Q2MC27;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Phosphate regulon transcriptional regulatory protein PhoB;
GN Name=phoB; OrderedLocusNames=b0399, JW0389;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3537313; DOI=10.1016/0022-2836(86)90073-2;
RA Makino K., Shinagawa H., Amemura M., Nakata A.;
RT "Nucleotide sequence of the phoB gene, the positive regulatory gene for the
RT phosphate regulon of Escherichia coli K-12.";
RL J. Mol. Biol. 190:37-44(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-126, AND PHOSPHORYLATION AT
RP ASP-53.
RX PubMed=9878437; DOI=10.1006/jmbi.1998.2326;
RA Sola M., Gomis-Rueth F.-X., Serrano L., Gonzalez A., Coll M.;
RT "Three-dimensional crystal structure of the transcription factor PhoB
RT receiver domain.";
RL J. Mol. Biol. 285:675-687(1999).
RN [6]
RP STRUCTURE BY NMR OF 126-229.
RX PubMed=10653699; DOI=10.1006/jmbi.1999.3379;
RA Okamura H., Hanaoka S., Nagadoi A., Makino K., Nishimura Y.;
RT "Structural comparison of the PhoB and OmpR DNA-binding/transactivation
RT domains and the arrangement of PhoB molecules on the phosphate box.";
RL J. Mol. Biol. 295:1225-1236(2000).
CC -!- FUNCTION: This protein is a positive regulator for the phosphate
CC regulon. Transcription of this operon is positively regulated by PhoB
CC and PhoR when phosphate is limited.
CC -!- INTERACTION:
CC P0AFJ5; P0AFJ5: phoB; NbExp=9; IntAct=EBI-1116564, EBI-1116564;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated by PhoR or CreC. {ECO:0000269|PubMed:9878437}.
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DR EMBL; X04026; CAA27659.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18123.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73502.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76179.1; -; Genomic_DNA.
DR PIR; A24256; RGECFB.
DR RefSeq; NP_414933.1; NC_000913.3.
DR RefSeq; WP_000113933.1; NZ_STEB01000007.1.
DR PDB; 1B00; X-ray; 1.88 A; A/B=1-127.
DR PDB; 1GXP; X-ray; 2.50 A; A/B/E/F=124-229.
DR PDB; 1GXQ; X-ray; 2.00 A; A=124-229.
DR PDB; 1QQI; NMR; -; A=126-229.
DR PDB; 1ZES; X-ray; 1.90 A; A/B/C=1-125.
DR PDB; 2IYN; X-ray; 2.08 A; A/B/C=1-127.
DR PDB; 2JB9; X-ray; 1.70 A; A/B=1-127.
DR PDB; 2JBA; X-ray; 1.45 A; A/B=1-127.
DR PDB; 2Z33; NMR; -; A=126-229.
DR PDB; 3T72; X-ray; 4.33 A; 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.
DR PDBsum; 1B00; -.
DR PDBsum; 1GXP; -.
DR PDBsum; 1GXQ; -.
DR PDBsum; 1QQI; -.
DR PDBsum; 1ZES; -.
DR PDBsum; 2IYN; -.
DR PDBsum; 2JB9; -.
DR PDBsum; 2JBA; -.
DR PDBsum; 2Z33; -.
DR PDBsum; 3T72; -.
DR AlphaFoldDB; P0AFJ5; -.
DR BMRB; P0AFJ5; -.
DR SMR; P0AFJ5; -.
DR BioGRID; 4259816; 27.
DR BioGRID; 849435; 5.
DR DIP; DIP-35852N; -.
DR IntAct; P0AFJ5; 24.
DR STRING; 511145.b0399; -.
DR jPOST; P0AFJ5; -.
DR PaxDb; P0AFJ5; -.
DR PRIDE; P0AFJ5; -.
DR EnsemblBacteria; AAC73502; AAC73502; b0399.
DR EnsemblBacteria; BAE76179; BAE76179; BAE76179.
DR GeneID; 67416528; -.
DR GeneID; 945046; -.
DR KEGG; ecj:JW0389; -.
DR KEGG; eco:b0399; -.
DR PATRIC; fig|1411691.4.peg.1879; -.
DR EchoBASE; EB0721; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_6; -.
DR InParanoid; P0AFJ5; -.
DR OMA; IDRVWGS; -.
DR PhylomeDB; P0AFJ5; -.
DR BioCyc; EcoCyc:PHOB-MON; -.
DR EvolutionaryTrace; P0AFJ5; -.
DR PRO; PR:P0AFJ5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0001108; F:bacterial-type RNA polymerase holo enzyme binding; IMP:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR011879; Sig_transdc_resp-reg_PhoB.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR TIGRFAMs; TIGR02154; PhoB; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Phosphate transport;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transport; Two-component regulatory system.
FT CHAIN 1..229
FT /note="Phosphate regulon transcriptional regulatory protein
FT PhoB"
FT /id="PRO_0000081186"
FT DOMAIN 4..120
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 129..227
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:9878437"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2JBA"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:2JBA"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2JBA"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:2JBA"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2JBA"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:2JBA"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:2JBA"
FT TURN 72..76
FT /evidence="ECO:0007829|PDB:2JBA"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2JBA"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2JBA"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2IYN"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2JBA"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:2JBA"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1GXQ"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1GXQ"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1GXQ"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1GXQ"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1GXP"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:1GXQ"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1GXQ"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:1GXQ"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1GXQ"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:1GXQ"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1GXQ"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:1GXQ"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1GXQ"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1GXQ"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1GXQ"
SQ SEQUENCE 229 AA; 26433 MW; EB46BA282F1F2C23 CRC64;
MARRILVVED EAPIREMVCF VLEQNGFQPV EAEDYDSAVN QLNEPWPDLI LLDWMLPGGS
GIQFIKHLKR ESMTRDIPVV MLTARGEEED RVRGLETGAD DYITKPFSPK ELVARIKAVM
RRISPMAVEE VIEMQGLSLD PTSHRVMAGE EPLEMGPTEF KLLHFFMTHP ERVYSREQLL
NHVWGTNVYV EDRTVDVHIR RLRKALEPGG HDRMVQTVRG TGYRFSTRF
