PHOE_ECOLI
ID PHOE_ECOLI Reviewed; 351 AA.
AC P02932;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Outer membrane porin PhoE;
DE AltName: Full=Outer membrane pore protein E;
DE Flags: Precursor;
GN Name=phoE; Synonyms=ompE; OrderedLocusNames=b0241, JW0231;
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=6341601; DOI=10.1016/0022-2836(83)90110-9;
RA Overbeeke N., Bergmans H., van Mansfeld F., Lugtenberg B.;
RT "Complete nucleotide sequence of phoE, the structural gene for the
RT phosphate limitation inducible outer membrane pore protein of Escherichia
RT coli K12.";
RL J. Mol. Biol. 163:513-532(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=6089111; DOI=10.1093/nar/12.15.6337;
RA Deutch A.H., Rushlow K.E., Smith C.J.;
RT "Analysis of the Escherichia coli proBA locus by DNA and protein
RT sequencing.";
RL Nucleic Acids Res. 12:6337-6355(1984).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION BY PHOSPHATE STARVATION.
RC STRAIN=K12 / JF568;
RX PubMed=2464593; DOI=10.1016/s0021-9258(19)81685-x;
RA Gehring K.B., Nikaido H.;
RT "Existence and purification of porin heterotrimers of Escherichia coli K12
RT OmpC, OmpF, and PhoE proteins.";
RL J. Biol. Chem. 264:2810-2815(1989).
RN [8]
RP MUTAGENESIS OF PHE-351.
RX PubMed=1848301; DOI=10.1016/0022-2836(91)90880-f;
RA Struyve M., Moons M., Tommassen J.;
RT "Carboxy-terminal phenylalanine is essential for the correct assembly of a
RT bacterial outer membrane protein.";
RL J. Mol. Biol. 218:141-148(1991).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
RX PubMed=1848682; DOI=10.1038/350167a0;
RA Jap B.K., Walian P.J., Gehring K.;
RT "Structural architecture of an outer membrane channel as determined by
RT electron crystallography.";
RL Nature 350:167-170(1991).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=1380671; DOI=10.1038/358727a0;
RA Cowan S.W., Schirmer T., Rummel G., Steiert M., Ghosh R., Pauptit R.A.,
RA Jansonius J.N., Rosenbusch J.P.;
RT "Crystal structures explain functional properties of two E. coli porins.";
RL Nature 358:727-733(1992).
RN [12]
RP TOPOLOGY.
RX PubMed=7679770; DOI=10.1111/j.1365-2958.1993.tb01104.x;
RA Struyve M., Visser J., Adriaanse H., Benz R., Tommassen J.;
RT "Topology of PhoE porin: the 'eyelet' region.";
RL Mol. Microbiol. 7:131-140(1993).
CC -!- FUNCTION: Uptake of inorganic phosphate, phosphorylated compounds, and
CC some other negatively charged solutes.
CC -!- SUBUNIT: Homotrimer (PubMed:2464593). Forms mixed heterotrimers with
CC OmpC and with OmpF; other mixed heterotrimers are also probable
CC (PubMed:2464593). {ECO:0000269|PubMed:2464593}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2464593};
CC Multi-pass membrane protein.
CC -!- INDUCTION: By phosphate starvation. {ECO:0000269|PubMed:2464593}.
CC -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR EMBL; V00316; CAA23605.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08661.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73345.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77910.1; -; Genomic_DNA.
DR EMBL; X00786; CAA25362.1; -; Genomic_DNA.
DR PIR; A03432; MMECPE.
DR RefSeq; NP_414776.1; NC_000913.3.
DR RefSeq; WP_000749863.1; NZ_LN832404.1.
DR PDB; 1PHO; X-ray; 3.00 A; A=22-351.
DR PDBsum; 1PHO; -.
DR AlphaFoldDB; P02932; -.
DR SMR; P02932; -.
DR BioGRID; 4259766; 264.
DR DIP; DIP-10498N; -.
DR IntAct; P02932; 4.
DR STRING; 511145.b0241; -.
DR TCDB; 1.B.1.1.2; the general bacterial porin (gbp) family.
DR SWISS-2DPAGE; P02932; -.
DR PaxDb; P02932; -.
DR PRIDE; P02932; -.
DR EnsemblBacteria; AAC73345; AAC73345; b0241.
DR EnsemblBacteria; BAA77910; BAA77910; BAA77910.
DR GeneID; 944926; -.
DR KEGG; ecj:JW0231; -.
DR KEGG; eco:b0241; -.
DR PATRIC; fig|1411691.4.peg.2042; -.
DR EchoBASE; EB0722; -.
DR eggNOG; COG3203; Bacteria.
DR HOGENOM; CLU_058202_0_0_6; -.
DR InParanoid; P02932; -.
DR OMA; KAMHYIS; -.
DR PhylomeDB; P02932; -.
DR BioCyc; EcoCyc:MON0-282; -.
DR BioCyc; MetaCyc:MON0-282; -.
DR EvolutionaryTrace; P02932; -.
DR PRO; PR:P02932; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IDA:CACAO.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0034220; P:ion transmembrane transport; IEA:InterPro.
DR CDD; cd00342; gram_neg_porins; 1.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR033900; Gram_neg_porin_domain.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR001897; Porin_gammaproteobac.
DR InterPro; IPR001702; Porin_Gram-ve.
DR InterPro; IPR013793; Porin_Gram-ve_CS.
DR Pfam; PF00267; Porin_1; 1.
DR PRINTS; PR00183; ECOLIPORIN.
DR PRINTS; PR00182; ECOLNEIPORIN.
DR PROSITE; PS00576; GRAM_NEG_PORIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Ion transport; Membrane; Porin;
KW Reference proteome; Signal; Stress response; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT CHAIN 22..351
FT /note="Outer membrane porin PhoE"
FT /id="PRO_0000025242"
FT MUTAGEN 351
FT /note="F->Y,N,S,V: Less resistant to trypsin."
FT /evidence="ECO:0000269|PubMed:1848301"
FT STRAND 28..49
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 68..85
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 93..104
FT /evidence="ECO:0007829|PDB:1PHO"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:1PHO"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1PHO"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1PHO"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:1PHO"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:1PHO"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:1PHO"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 225..239
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 263..274
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 277..294
FT /evidence="ECO:0007829|PDB:1PHO"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 301..327
FT /evidence="ECO:0007829|PDB:1PHO"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:1PHO"
SQ SEQUENCE 351 AA; 38922 MW; 249E2E362C030C9A CRC64;
MKKSTLALVV MGIVASASVQ AAEIYNKDGN KLDVYGKVKA MHYMSDNASK DGDQSYIRFG
FKGETQINDQ LTGYGRWEAE FAGNKAESDT AQQKTRLAFA GLKYKDLGSF DYGRNLGALY
DVEAWTDMFP EFGGDSSAQT DNFMTKRASG LATYRNTDFF GVIDGLNLTL QYQGKNENRD
VKKQNGDGFG TSLTYDFGGS DFAISGAYTN SDRTNEQNLQ SRGTGKRAEA WATGLKYDAN
NIYLATFYSE TRKMTPITGG FANKTQNFEA VAQYQFDFGL RPSLGYVLSK GKDIEGIGDE
DLVNYIDVGA TYYFNKNMSA FVDYKINQLD SDNKLNINND DIVAVGMTYQ F
