OMPF_ECOLI
ID OMPF_ECOLI Reviewed; 362 AA.
AC P02931;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Outer membrane porin F;
DE AltName: Full=Outer membrane protein 1A;
DE AltName: Full=Outer membrane protein B;
DE AltName: Full=Outer membrane protein F;
DE AltName: Full=Outer membrane protein IA;
DE AltName: Full=Porin OmpF;
DE Flags: Precursor;
GN Name=ompF; Synonyms=cmlB, coa, cry, tolF; OrderedLocusNames=b0929, JW0912;
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=6294623; DOI=10.1093/nar/10.21.6957;
RA Inokuchi K., Mutoh N., Matsuyama S., Mizushima S.;
RT "Primary structure of the ompF gene that codes for a major outer membrane
RT protein of Escherichia coli K-12.";
RL Nucleic Acids Res. 10:6957-6968(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RC STRAIN=K12;
RX PubMed=7037455; DOI=10.1016/0014-5793(82)80341-4;
RA Mutoh N., Inokuchi K., Mizushima S.;
RT "Amino acid sequence of the signal peptide of OmpF, a major outer membrane
RT protein of Escherichia coli.";
RL FEBS Lett. 137:171-174(1982).
RN [6]
RP PROTEIN SEQUENCE OF 23-362.
RC STRAIN=B/r;
RX PubMed=7049161; DOI=10.1042/bj2030033;
RA Chen R., Kramer C., Schmidmayr W., Chen-Schmeisser U., Henning U.;
RT "Primary structure of major outer-membrane protein I (ompF protein, porin)
RT of Escherichia coli B/r.";
RL Biochem. J. 203:33-43(1982).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-63.
RX PubMed=2997131; DOI=10.1128/jb.164.2.797-801.1985;
RA Nogami T., Mizuno T., Mizushima S.;
RT "Construction of a series of ompF-ompC chimeric genes by in vivo homologous
RT recombination in Escherichia coli and characterization of the translational
RT products.";
RL J. Bacteriol. 164:797-801(1985).
RN [8]
RP PROTEIN SEQUENCE OF 23-34 AND 39-47.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 23-27.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9629924; DOI=10.1002/elps.1150190539;
RA Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M.,
RA Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
RT "Extraction of membrane proteins by differential solubilization for
RT separation using two-dimensional gel electrophoresis.";
RL Electrophoresis 19:837-844(1998).
RN [10]
RP INDUCTION BY LOW OSMOLARITY.
RC STRAIN=K12;
RX PubMed=3010044; DOI=10.1007/bf00331636;
RA Nara F., Matsuyama S., Mizuno T., Mizushima S.;
RT "Molecular analysis of mutant ompR genes exhibiting different phenotypes as
RT to osmoregulation of the ompF and ompC genes of Escherichia coli.";
RL Mol. Gen. Genet. 202:194-199(1986).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION BY LOW OSMOLARITY.
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 [12]
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 [13]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [14]
RP ROLE IN ANTIBIOTIC SUSCEPTIBILITY, INDUCTION, REGULATION BY LON/YCGE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / AG100;
RX PubMed=19721064; DOI=10.1128/aac.00787-09;
RA Duval V., Nicoloff H., Levy S.B.;
RT "Combined inactivation of lon and ycgE decreases multidrug susceptibility
RT by reducing the amount of OmpF porin in Escherichia coli.";
RL Antimicrob. Agents Chemother. 53:4944-4948(2009).
RN [15]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=27723824; DOI=10.1371/journal.ppat.1005925;
RA Beck C.M., Willett J.L., Cunningham D.A., Kim J.J., Low D.A., Hayes C.S.;
RT "CdiA effectors from uropathogenic Escherichia coli use heterotrimeric
RT osmoporins as receptors to recognize target bacteria.";
RL PLoS Pathog. 12:E1005925-E1005925(2016).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.4 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 [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT ASP-141.
RX PubMed=7524100; DOI=10.1073/pnas.91.22.10675;
RA Jeanteur D., Schirmer T., Fourel D., Simonet V., Rummel G., Widmer C.,
RA Rosenbusch J.P., Pattus F., Pages J.-M.;
RT "Structural and functional alterations of a colicin-resistant mutant of
RT OmpF porin from Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:10675-10679(1994).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9843370; DOI=10.1021/bi981215c;
RA Phale P.S., Philippsen A., Kiefhaber T., Koebnik R., Phale V.P.,
RA Schirmer T., Rosenbusch J.P.;
RT "Stability of trimeric OmpF porin: the contributions of the latching loop
RT L2.";
RL Biochemistry 37:15663-15670(1998).
CC -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC across the outer membrane. {ECO:0000305|PubMed:19721064}.
CC -!- FUNCTION: (Microbial infection) It is also a receptor for the
CC bacteriophage T2. Is the major receptor for colicin E5 (Probable).
CC {ECO:0000305|PubMed:27723824}.
CC -!- FUNCTION: (Microbial infection) A mixed OmpC-OmpF heterotrimer is the
CC outer membrane receptor for toxin CdiA-EC536; polymorphisms in
CC extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-
CC EC536-mediated toxicity. {ECO:0000269|PubMed:27723824}.
CC -!- SUBUNIT: Homotrimer (PubMed:2464593, PubMed:16079137). Forms mixed
CC heterotrimers with OmpC and with PhoE; other mixed heterotrimers are
CC also probable (PubMed:2464593). {ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:2464593}.
CC -!- INTERACTION:
CC P02931; P76506: mlaA; NbExp=4; IntAct=EBI-371336, EBI-1128511;
CC P02931; P02931: ompF; NbExp=7; IntAct=EBI-371336, EBI-371336;
CC P02931; P08083: cna; Xeno; NbExp=3; IntAct=EBI-371336, EBI-15691934;
CC P02931; P09883: col; Xeno; NbExp=4; IntAct=EBI-371336, EBI-1029888;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:2464593}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: By growth in low osmolarity conditions (low sugar or salt);
CC activated at low osmolarity by OmpR, repressed at high osmolarity by
CC OmpR (at protein level) (PubMed:3010044, PubMed:2464593). Levels of
CC OmpF protein decrease in a lon/ycgE double disruption (at protein
CC level) (PubMed:19721064). {ECO:0000269|PubMed:19721064,
CC ECO:0000269|PubMed:2464593, ECO:0000269|PubMed:3010044}.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased susceptibility to a number of
CC hydrophilic antibiotics including ampicillin, cefoxitin and
CC tetracycline (PubMed:19721064). Deletion of ompF confers resistance to
CC colicin E5 (PubMed:27723824). {ECO:0000269|PubMed:19721064,
CC ECO:0000269|PubMed:27723824}.
CC -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR EMBL; J01655; AAA24244.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74015.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35675.1; -; Genomic_DNA.
DR PIR; A93449; MMECF.
DR RefSeq; NP_415449.1; NC_000913.3.
DR RefSeq; WP_000977920.1; NZ_STEB01000006.1.
DR PDB; 1BT9; X-ray; 3.00 A; A=23-362.
DR PDB; 1GFM; X-ray; 3.50 A; A=23-362.
DR PDB; 1GFN; X-ray; 3.10 A; A=23-362.
DR PDB; 1GFO; X-ray; 3.30 A; A=23-362.
DR PDB; 1GFP; X-ray; 2.70 A; A=23-362.
DR PDB; 1GFQ; X-ray; 2.80 A; A=23-362.
DR PDB; 1HXT; X-ray; 2.40 A; A=23-362.
DR PDB; 1HXU; X-ray; 3.00 A; A=23-362.
DR PDB; 1HXX; X-ray; 2.20 A; A=23-362.
DR PDB; 1MPF; X-ray; 3.00 A; A=23-362.
DR PDB; 1OPF; X-ray; 3.20 A; A/B/C/D/E/F=23-362.
DR PDB; 2OMF; X-ray; 2.40 A; A=23-362.
DR PDB; 2ZFG; X-ray; 1.59 A; A=23-362.
DR PDB; 2ZLD; X-ray; 3.00 A; A/B=23-362.
DR PDB; 3FYX; X-ray; 3.40 A; A=23-362.
DR PDB; 3HW9; X-ray; 2.61 A; A/B=1-362.
DR PDB; 3HWB; X-ray; 3.00 A; A/B=1-362.
DR PDB; 3K19; X-ray; 3.79 A; A/B/C/D/E/F/G/H/I/J/K/L=23-362.
DR PDB; 3K1B; X-ray; 4.39 A; A/B/C/D=23-362.
DR PDB; 3O0E; X-ray; 3.01 A; A/B/C/D/E/F=23-362.
DR PDB; 3POQ; X-ray; 1.90 A; A=23-362.
DR PDB; 3POU; X-ray; 2.80 A; A=23-362.
DR PDB; 3POX; X-ray; 2.00 A; A/B/C/D/E/F=23-362.
DR PDB; 4D5U; X-ray; 3.50 A; A/B/C/D/E/F=23-362.
DR PDB; 4GCP; X-ray; 1.98 A; A/B=23-362.
DR PDB; 4GCQ; X-ray; 2.20 A; A/B=23-362.
DR PDB; 4GCS; X-ray; 1.87 A; A/B=23-362.
DR PDB; 4JFB; X-ray; 3.80 A; A/B/C/D/E/F=23-362.
DR PDB; 4LSE; X-ray; 2.10 A; A/B/C=23-362.
DR PDB; 4LSF; X-ray; 1.90 A; A/B=23-362.
DR PDB; 4LSH; X-ray; 2.20 A; A/B=23-362.
DR PDB; 4LSI; X-ray; 2.09 A; A/B/C=23-362.
DR PDB; 5NUO; X-ray; 3.20 A; A/C/E=23-362.
DR PDB; 5NUQ; X-ray; 3.20 A; A/B/C/D/E/F=23-362.
DR PDB; 5NUR; X-ray; 3.29 A; A/C/E=23-362.
DR PDB; 6WTZ; EM; 3.15 A; A/B/C=1-362.
DR PDB; 6ZHP; X-ray; 2.05 A; B=1-362.
DR PDB; 6ZHV; X-ray; 1.95 A; A/B/C=1-362.
DR PDB; 7NST; EM; 3.70 A; A/B/C=23-362.
DR PDB; 7NSU; EM; 4.70 A; A/B/C=23-362.
DR PDBsum; 1BT9; -.
DR PDBsum; 1GFM; -.
DR PDBsum; 1GFN; -.
DR PDBsum; 1GFO; -.
DR PDBsum; 1GFP; -.
DR PDBsum; 1GFQ; -.
DR PDBsum; 1HXT; -.
DR PDBsum; 1HXU; -.
DR PDBsum; 1HXX; -.
DR PDBsum; 1MPF; -.
DR PDBsum; 1OPF; -.
DR PDBsum; 2OMF; -.
DR PDBsum; 2ZFG; -.
DR PDBsum; 2ZLD; -.
DR PDBsum; 3FYX; -.
DR PDBsum; 3HW9; -.
DR PDBsum; 3HWB; -.
DR PDBsum; 3K19; -.
DR PDBsum; 3K1B; -.
DR PDBsum; 3O0E; -.
DR PDBsum; 3POQ; -.
DR PDBsum; 3POU; -.
DR PDBsum; 3POX; -.
DR PDBsum; 4D5U; -.
DR PDBsum; 4GCP; -.
DR PDBsum; 4GCQ; -.
DR PDBsum; 4GCS; -.
DR PDBsum; 4JFB; -.
DR PDBsum; 4LSE; -.
DR PDBsum; 4LSF; -.
DR PDBsum; 4LSH; -.
DR PDBsum; 4LSI; -.
DR PDBsum; 5NUO; -.
DR PDBsum; 5NUQ; -.
DR PDBsum; 5NUR; -.
DR PDBsum; 6WTZ; -.
DR PDBsum; 6ZHP; -.
DR PDBsum; 6ZHV; -.
DR PDBsum; 7NST; -.
DR PDBsum; 7NSU; -.
DR AlphaFoldDB; P02931; -.
DR SMR; P02931; -.
DR BioGRID; 4260018; 306.
DR BioGRID; 849928; 1.
DR DIP; DIP-10398N; -.
DR IntAct; P02931; 9.
DR MINT; P02931; -.
DR STRING; 511145.b0929; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB13092; Meclocycline.
DR DrugBank; DB01017; Minocycline.
DR DrugBank; DB07084; N-(6,7,9,10,17,18,20,21-octahydrodibenzo[b,k][1,4,7,10,13,16]hexaoxacyclooctadecin-2-yl)acetamide.
DR TCDB; 1.B.1.1.1; the general bacterial porin (gbp) family.
DR SWISS-2DPAGE; P02931; -.
DR jPOST; P02931; -.
DR PaxDb; P02931; -.
DR PRIDE; P02931; -.
DR EnsemblBacteria; AAC74015; AAC74015; b0929.
DR EnsemblBacteria; BAA35675; BAA35675; BAA35675.
DR GeneID; 66670795; -.
DR GeneID; 945554; -.
DR KEGG; ecj:JW0912; -.
DR KEGG; eco:b0929; -.
DR PATRIC; fig|1411691.4.peg.1347; -.
DR EchoBASE; EB0665; -.
DR eggNOG; COG3203; Bacteria.
DR HOGENOM; CLU_058202_0_0_6; -.
DR InParanoid; P02931; -.
DR OMA; DAIGWTD; -.
DR PhylomeDB; P02931; -.
DR BioCyc; EcoCyc:EG10671-MON; -.
DR BioCyc; MetaCyc:EG10671-MON; -.
DR EvolutionaryTrace; P02931; -.
DR PHI-base; PHI:7023; -.
DR PRO; PR:P02931; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:CAFA.
DR GO; GO:0034702; C:ion channel complex; IDA:CAFA.
DR GO; GO:0046930; C:pore complex; IDA:EcoCyc.
DR GO; GO:0042912; F:colicin transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0005216; F:ion channel activity; IDA:CAFA.
DR GO; GO:0008289; F:lipid binding; IDA:EcoCyc.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:EcoCyc.
DR GO; GO:0015288; F:porin activity; IMP:EcoliWiki.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:CAFA.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:CAFA.
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; Direct protein sequencing;
KW Ion transport; Membrane; Porin; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:7049161,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9629924"
FT CHAIN 23..362
FT /note="Outer membrane porin F"
FT /id="PRO_0000025237"
FT TRANSMEM 23..28
FT /note="Beta stranded"
FT TOPO_DOM 29
FT /note="Periplasmic"
FT TRANSMEM 30..45
FT /note="Beta stranded"
FT TOPO_DOM 46..60
FT /note="Extracellular"
FT TRANSMEM 61..73
FT /note="Beta stranded"
FT TOPO_DOM 74..75
FT /note="Periplasmic"
FT TRANSMEM 76..88
FT /note="Beta stranded"
FT TOPO_DOM 89..104
FT /note="Extracellular"
FT TRANSMEM 105..113
FT /note="Beta stranded"
FT TOPO_DOM 114..115
FT /note="Periplasmic"
FT TRANSMEM 116..122
FT /note="Beta stranded"
FT TOPO_DOM 123..156
FT /note="Extracellular"
FT TRANSMEM 157..163
FT /note="Beta stranded"
FT TOPO_DOM 164..171
FT /note="Periplasmic"
FT TRANSMEM 172..181
FT /note="Beta stranded"
FT TOPO_DOM 182..193
FT /note="Extracellular"
FT TRANSMEM 194..204
FT /note="Beta stranded"
FT TOPO_DOM 205
FT /note="Periplasmic"
FT TRANSMEM 206..217
FT /note="Beta stranded"
FT TOPO_DOM 218..232
FT /note="Extracellular"
FT TRANSMEM 233..244
FT /note="Beta stranded"
FT TOPO_DOM 245
FT /note="Periplasmic"
FT TRANSMEM 246..257
FT /note="Beta stranded"
FT TOPO_DOM 258..274
FT /note="Extracellular"
FT TRANSMEM 275..287
FT /note="Beta stranded"
FT TOPO_DOM 288..289
FT /note="Periplasmic"
FT TRANSMEM 290..303
FT /note="Beta stranded"
FT TOPO_DOM 304..313
FT /note="Extracellular"
FT TRANSMEM 314..325
FT /note="Beta stranded"
FT TOPO_DOM 326..327
FT /note="Periplasmic"
FT TRANSMEM 328..337
FT /note="Beta stranded"
FT TOPO_DOM 338..352
FT /note="Extracellular"
FT TRANSMEM 353..362
FT /note="Beta stranded"
FT VARIANT 88
FT /note="Q -> E (in strain: B/r; AA sequence)"
FT /evidence="ECO:0000305"
FT VARIANT 139
FT /note="E -> G (in strain: B/r; AA sequence)"
FT /evidence="ECO:0000305"
FT VARIANT 284
FT /note="Q -> L (in strain: B/r; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 31..45
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1HXX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 74..91
FT /evidence="ECO:0007829|PDB:2ZFG"
FT TURN 95..100
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 102..112
FT /evidence="ECO:0007829|PDB:2ZFG"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:2ZFG"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2ZFG"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4LSI"
FT STRAND 152..164
FT /evidence="ECO:0007829|PDB:2ZFG"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 207..217
FT /evidence="ECO:0007829|PDB:2ZFG"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 231..244
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 247..258
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2ZFG"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 274..285
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 290..305
FT /evidence="ECO:0007829|PDB:2ZFG"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 309..326
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:2ZFG"
FT STRAND 353..362
FT /evidence="ECO:0007829|PDB:2ZFG"
SQ SEQUENCE 362 AA; 39333 MW; 3F0974D96DB65464 CRC64;
MMKRNILAVI VPALLVAGTA NAAEIYNKDG NKVDLYGKAV GLHYFSKGNG ENSYGGNGDM
TYARLGFKGE TQINSDLTGY GQWEYNFQGN NSEGADAQTG NKTRLAFAGL KYADVGSFDY
GRNYGVVYDA LGYTDMLPEF GGDTAYSDDF FVGRVGGVAT YRNSNFFGLV DGLNFAVQYL
GKNERDTARR SNGDGVGGSI SYEYEGFGIV GAYGAADRTN LQEAQPLGNG KKAEQWATGL
KYDANNIYLA ANYGETRNAT PITNKFTNTS GFANKTQDVL LVAQYQFDFG LRPSIAYTKS
KAKDVEGIGD VDLVNYFEVG ATYYFNKNMS TYVDYIINQI DSDNKLGVGS DDTVAVGIVY
QF
