OMPA_ECOLI
ID OMPA_ECOLI Reviewed; 346 AA.
AC P0A910; P02934;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Outer membrane protein A {ECO:0000255|HAMAP-Rule:MF_00842, ECO:0000303|PubMed:791936};
DE Short=OmpA;
DE AltName: Full=Outer membrane porin A {ECO:0000255|HAMAP-Rule:MF_00842};
DE AltName: Full=Outer membrane protein 3A {ECO:0000303|PubMed:1107069};
DE AltName: Full=Outer membrane protein B;
DE AltName: Full=Outer membrane protein II*;
DE AltName: Full=Outer membrane protein d;
DE Flags: Precursor;
GN Name=ompA {ECO:0000255|HAMAP-Rule:MF_00842, ECO:0000303|PubMed:791936};
GN Synonyms=con {ECO:0000303|PubMed:4604263},
GN tolG {ECO:0000303|PubMed:4591955}, tut {ECO:0000303|PubMed:1107069};
GN OrderedLocusNames=b0957, JW0940;
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=6253901; DOI=10.1093/nar/8.13.3011;
RA Beck E., Bremer E.;
RT "Nucleotide sequence of the gene ompA coding the outer membrane protein II
RT of Escherichia coli K-12.";
RL Nucleic Acids Res. 8:3011-3027(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6260961; DOI=10.1016/0022-2836(80)90193-x;
RA Movva N.R., Nakamura K., Inouye M.;
RT "Gene structure of the OmpA protein, a major surface protein of Escherichia
RT coli required for cell-cell interaction.";
RL J. Mol. Biol. 143:317-328(1980).
RN [3]
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 [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 PROTEIN SEQUENCE OF 22-346.
RC STRAIN=K12;
RX PubMed=7001461; DOI=10.1073/pnas.77.8.4592;
RA Chen R., Schmidmayr W., Kramer C., Chen-Schmeisser U., Henning U.;
RT "Primary structure of major outer membrane protein II* (ompA protein) of
RT Escherichia coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:4592-4596(1980).
RN [7]
RP PROTEIN SEQUENCE OF 22-34.
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 [8]
RP PROTEIN SEQUENCE OF 22-32.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 22-26.
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 PROTEIN SEQUENCE OF 183-195, HYDROXYBUTYRYLATION AT SER-184 AND SER-188,
RP AND MUTAGENESIS OF 183-LEU--SER-188; 184-SER--VAL-187; SER-184;
RP 185-LEU--SER-188; SER-188; TYR-189 AND ARG-190.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=17659252; DOI=10.1016/j.bbamem.2007.06.019;
RA Xian M., Fuerst M.M., Shabalin Y., Reusch R.N.;
RT "Sorting signal of Escherichia coli OmpA is modified by oligo-(R)-3-
RT hydroxybutyrate.";
RL Biochim. Biophys. Acta 1768:2660-2666(2007).
RN [11]
RP PROTEIN SEQUENCE OF 289-298 AND 336-346, AND DIMERIZATION.
RX PubMed=21697552; DOI=10.1074/mcp.m110.006841;
RA Zheng C., Yang L., Hoopmann M.R., Eng J.K., Tang X., Weisbrod C.R.,
RA Bruce J.E.;
RT "Cross-linking measurements of in vivo protein complex topologies.";
RL Mol. Cell. Proteomics 10:M110.006841-M110.006841(2011).
RN [12]
RP FUNCTION IN CONJUGATION, AND FUNCTION IN SUSCEPTIBILITY TO PHAGE (MICROBIAL
RP INFECTION).
RC STRAIN=K12;
RX PubMed=4604263; DOI=10.1128/jb.119.3.726-735.1974;
RA Skurray R.A., Hancock R.E., Reeves P.;
RT "Con- mutants: class of mutants in Escherichia coli K-12 lacking a major
RT cell wall protein and defective in conjugation and adsorption of a
RT bacteriophage.";
RL J. Bacteriol. 119:726-735(1974).
RN [13]
RP FUNCTION IN TOLERANCE TO BACTERIOCIN JF246 (MICROBIAL INFECTION), AND GENE
RP NAME.
RC STRAIN=K12;
RX PubMed=4591955; DOI=10.1128/jb.117.3.1354-1355.1974;
RA Foulds J.;
RT "Chromosomal location of the tolG locus for tolerance to bacteriocin JF246
RT in Escherichia coli K-12.";
RL J. Bacteriol. 117:1354-1355(1974).
RN [14]
RP FUNCTION IN SUSCEPTIBILITY TO BACTERIOPHAGE TUII* (MICROBIAL INFECTION),
RP AND GENE IDENTIFICATION.
RX PubMed=1107069; DOI=10.1016/0014-5793(76)80168-8;
RA Henning U., Hindennach I., Haller I.;
RT "The major proteins of the Escherichia coli outer cell envelope membrane:
RT evidence for the structural gene of protein II.";
RL FEBS Lett. 61:46-48(1976).
RN [15]
RP GENE NAME, FUNCTION IN SUSCEPTIBILITY TO BACTERIOPHAGE TUII* (MICROBIAL
RP INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=791936; DOI=10.1128/jb.128.3.834-841.1976;
RA Datta D.B., Kraemer C., Henning U.;
RT "Diploidy for a structural gene specifying a major protein of the outer
RT cell envelope membrane from Escherichia coli K-12.";
RL J. Bacteriol. 128:834-841(1976).
RN [16]
RP FUNCTION IN SUSCEPTIBILITY TO BACTERIOPHAGES (MICROBIAL INFECTION).
RC STRAIN=K12 / P400;
RX PubMed=783129; DOI=10.1128/jb.127.3.1080-1084.1976;
RA Manning P.A., Puspurs A., Reeves P.;
RT "Outer membrane of Escherichia coli K-12: isolation of mutants with altered
RT protein 3A by using host range mutants of bacteriophage K3.";
RL J. Bacteriol. 127:1080-1084(1976).
RN [17]
RP ISOLATED PROTEIN INHIBITS CONJUGATION.
RC STRAIN=K12;
RX PubMed=321438; DOI=10.1128/jb.129.3.1651-1652.1977;
RA Schweizer M., Henning U.;
RT "Action of a major outer cell envelope membrane protein in conjugation of
RT Escherichia coli K-12.";
RL J. Bacteriol. 129:1651-1652(1977).
RN [18]
RP MUTANTS ALTER OUTER MEMBRANE SHAPE AND INTEGRITY.
RX PubMed=361695; DOI=10.1128/jb.136.1.280-285.1978;
RA Sonntag I., Schwarz H., Hirota Y., Henning U.;
RT "Cell envelope and shape of Escherichia coli: multiple mutants missing the
RT outer membrane lipoprotein and other major outer membrane proteins.";
RL J. Bacteriol. 136:280-285(1978).
RN [19]
RP FUNCTION (MICROBIAL INFECTION), MUTANTS SENSITIVE TO PHAGE, AND MUTAGENESIS
RP OF GLY-86; GLU-89; GLY-91; VAL-131; 126-ASP-THR-127 AND GLY-175.
RC STRAIN=K12 / P400;
RX PubMed=6086577; DOI=10.1128/jb.159.2.570-578.1984;
RA Morona R., Klose M., Henning U.;
RT "Escherichia coli K-12 outer membrane protein (OmpA) as a bacteriophage
RT receptor: analysis of mutant genes expressing altered proteins.";
RL J. Bacteriol. 159:570-578(1984).
RN [20]
RP SUBUNIT, AND INTERACTION WITH LPP.
RC STRAIN=K12 / SM1006;
RX PubMed=3013869; DOI=10.1016/s0021-9258(19)84474-5;
RA Choi D.-S., Yamada H., Mizuno T., Mizushima S.;
RT "Trimeric structure and localization of the major lipoprotein in the cell
RT surface of Escherichia coli.";
RL J. Biol. Chem. 261:8953-8957(1986).
RN [21]
RP MUTANTS RESISTANT TO PHAGE ENTRY, AND MUTAGENESIS OF ILE-45; GLY-49;
RP GLY-86; GLU-89; GLY-91; SER-129; VAL-131 AND GLY-175.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=3902787; DOI=10.1128/jb.164.2.539-543.1985;
RA Morona R., Kramer C., Henning U.;
RT "Bacteriophage receptor area of outer membrane protein OmpA of Escherichia
RT coli K-12.";
RL J. Bacteriol. 164:539-543(1985).
RN [22]
RP DOMAIN, DISULFIDE BOND, AND MUTAGENESIS OF CYS-311.
RX PubMed=2211627; DOI=10.1016/s0021-9258(17)44908-8;
RA Tani K., Tokuda H., Mizushima S.;
RT "Translocation of ProOmpA possessing an intramolecular disulfide bridge
RT into membrane vesicles of Escherichia coli. Effect of membrane
RT energization.";
RL J. Biol. Chem. 265:17341-17347(1990).
RN [23]
RP PORIN ACTIVITY, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=1370823; DOI=10.1016/s0021-9258(18)45908-x;
RA Sugawara E., Nikaido H.;
RT "Pore-forming activity of OmpA protein of Escherichia coli.";
RL J. Biol. Chem. 267:2507-2511(1992).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=7813480; DOI=10.1111/j.1432-1033.1994.00891.x;
RA Kuhn A., Kiefer D., Koehne C., Zhu H.-Y., Tschantz W.R., Dalbey R.E.;
RT "Evidence for a loop-like insertion mechanism of pro-Omp A into the inner
RT membrane of Escherichia coli.";
RL Eur. J. Biochem. 226:891-897(1994).
RN [25]
RP TOPOLOGY.
RX PubMed=8106193; DOI=10.1111/j.1399-3011.1993.tb00149.x;
RA Gromiha M.M., Ponnuswamy P.K.;
RT "Prediction of transmembrane beta-strands from hydrophobic characteristics
RT of proteins.";
RL Int. J. Pept. Protein Res. 42:420-431(1993).
RN [26]
RP PORES HAVE OPEN AND CLOSED FORMS.
RC STRAIN=K12;
RX PubMed=7517935; DOI=10.1016/s0021-9258(17)32406-7;
RA Sugawara E., Nikaido H.;
RT "OmpA protein of Escherichia coli outer membrane occurs in open and closed
RT channel forms.";
RL J. Biol. Chem. 269:17981-17987(1994).
RN [27]
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 [28]
RP FUNCTION IN CONJUGATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=JC3272;
RX PubMed=9696748; DOI=10.1128/jb.180.16.4036-4043.1998;
RA Klimke W.A., Frost L.S.;
RT "Genetic analysis of the role of the transfer gene, traN, of the F and
RT R100-1 plasmids in mating pair stabilization during conjugation.";
RL J. Bacteriol. 180:4036-4043(1998).
RN [29]
RP FUNCTION IN CONJUGATION, FUNCTION IN PHAGE K3 INFECTION (MICROBIAL
RP INFECTION), AND TOPOLOGY.
RC STRAIN=UH300;
RX PubMed=10368142; DOI=10.1128/jb.181.12.3688-3694.1999;
RA Koebnik R.;
RT "Structural and functional roles of the surface-exposed loops of the beta-
RT barrel membrane protein OmpA from Escherichia coli.";
RL J. Bacteriol. 181:3688-3694(1999).
RN [30]
RP FUNCTION AS A PORIN, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=10636850; DOI=10.1074/jbc.275.3.1594;
RA Arora A., Rinehart D., Szabo G., Tamm L.K.;
RT "Refolded outer membrane protein A of Escherichia coli forms ion channels
RT with two conductance states in planar lipid bilayers.";
RL J. Biol. Chem. 275:1594-1600(2000).
RN [31]
RP DIGESTED BY HOST NEUTROPHIL ELASTASE (ELANE), SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=10947984; DOI=10.1126/science.289.5482.1185;
RA Belaaouaj A., Kim K.S., Shapiro S.D.;
RT "Degradation of outer membrane protein A in Escherichia coli killing by
RT neutrophil elastase.";
RL Science 289:1185-1188(2000).
RN [32]
RP FUNCTION, DISRUPTION PHENOTYPE, VARIANT VAL-114, AND MUTAGENESIS OF LYS-128
RP AND ASN-130.
RC STRAIN=K1 / E44;
RX PubMed=11906175; DOI=10.1006/bbrc.2002.6657;
RA Wang Y.;
RT "The function of OmpA in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 292:396-401(2002).
RN [33]
RP PORE FORMATION DEPENDS ON TEMPERATURE, AND DOMAIN.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=15850404; DOI=10.1021/bi047278e;
RA Zakharian E., Reusch R.N.;
RT "Kinetics of folding of Escherichia coli OmpA from narrow to large pore
RT conformation in a planar bilayer.";
RL Biochemistry 44:6701-6707(2005).
RN [34]
RP DIMERIZATION, AND SUBCELLULAR LOCATION.
RC STRAIN=B / 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 [35]
RP FUNCTION IN CONJUGATION, AND SUBUNIT.
RX PubMed=16272376; DOI=10.1099/mic.0.28025-0;
RA Klimke W.A., Rypien C.D., Klinger B., Kennedy R.A.,
RA Rodriguez-Maillard J.M., Frost L.S.;
RT "The mating pair stabilization protein, TraN, of the F plasmid is an outer-
RT membrane protein with two regions that are important for its function in
RT conjugation.";
RL Microbiology 151:3527-3540(2005).
RN [36]
RP FUNCTION AS A PORIN, GATING MECHANISM, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 73-GLU--LYS-103; GLU-73; LYS-103; GLU-149 AND ARG-159.
RX PubMed=17041590; DOI=10.1038/nchembio827;
RA Hong H., Szabo G., Tamm L.K.;
RT "Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for
RT pore opening.";
RL Nat. Chem. Biol. 2:627-635(2006).
RN [37]
RP FUNCTION, HYDROXYBUTYRYLATION AT SER-184 AND SER-188, AND MUTAGENESIS OF
RP SER-184 AND SER-188.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=20004640; DOI=10.1016/j.bbamem.2009.11.023;
RA Negoda A., Negoda E., Reusch R.N.;
RT "Oligo-(R)-3-hydroxybutyrate modification of sorting signal enables pore
RT formation by Escherichia coli OmpA.";
RL Biochim. Biophys. Acta 1798:1480-1484(2010).
RN [38]
RP FUNCTION, DOMAIN, HYDROXYBUTYRYLATION IN C-TERMINUS, AND DISULFIDE BOND.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=21069910; DOI=10.1111/j.1742-4658.2010.07823.x;
RA Negoda A., Negoda E., Reusch R.N.;
RT "Resolving the native conformation of Escherichia coli OmpA.";
RL FEBS J. 277:4427-4437(2010).
RN [39]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.m111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [40]
RP PROTEIN COPY NUMBER.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24766808; DOI=10.1016/j.cell.2014.02.033;
RA Li G.W., Burkhardt D., Gross C., Weissman J.S.;
RT "Quantifying absolute protein synthesis rates reveals principles underlying
RT allocation of cellular resources.";
RL Cell 157:624-635(2014).
RN [41]
RP DIMERIZATION, DOMAIN, AND MUTAGENESIS OF LYS-213; 248-LEU--ALA-346;
RP 298-ARG--ALA-346 AND LYS-338.
RX PubMed=24746938; DOI=10.1016/j.str.2014.03.004;
RA Marcoux J., Politis A., Rinehart D., Marshall D.P., Wallace M.I.,
RA Tamm L.K., Robinson C.V.;
RT "Mass spectrometry defines the C-terminal dimerization domain and enables
RT modeling of the structure of full-length OmpA.";
RL Structure 22:781-790(2014).
RN [42]
RP MODELING OF FUNCTION, DOMAIN, AND PEPTIDOGLYCAN-BINDING.
RX PubMed=27866852; DOI=10.1016/j.str.2016.10.009;
RA Samsudin F., Ortiz-Suarez M.L., Piggot T.J., Bond P.J., Khalid S.;
RT "OmpA: a flexible clamp for bacterial cell wall attachment.";
RL Structure 24:2227-2235(2016).
RN [43]
RP MODELING OF FUNCTION, DOMAIN, AND PEPTIDOGLYCAN-BINDING.
RX PubMed=28978443; DOI=10.1016/j.bpj.2017.08.011;
RA Samsudin F., Boags A., Piggot T.J., Khalid S.;
RT "Braun's lipoprotein facilitates OmpA interaction with the Escherichia coli
RT cell wall.";
RL Biophys. J. 113:1496-1504(2017).
RN [44]
RP MODELING OF FUNCTION, DOMAIN, AND PEPTIDOGLYCAN-BINDING.
RX PubMed=30713026; DOI=10.1016/j.str.2019.01.001;
RA Boags A.T., Samsudin F., Khalid S.;
RT "Binding from both sides: TolR and full-length OmpA bind and maintain the
RT local structure of the E. coli cell wall.";
RL Structure 27:713-724(2019).
RN [45] {ECO:0007744|PDB:1BXW}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-192, SUBUNIT, SUBCELLULAR
RP LOCATION, TOPOLOGY, AND MUTAGENESIS OF LYS-128.
RX PubMed=9808047; DOI=10.1038/2983;
RA Pautsch A., Schulz G.E.;
RT "Structure of the outer membrane protein A transmembrane domain.";
RL Nat. Struct. Biol. 5:1013-1017(1998).
RN [46] {ECO:0007744|PDB:1QJP}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 22-192, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10764596; DOI=10.1006/jmbi.2000.3671;
RA Pautsch A., Schulz G.E.;
RT "High-resolution structure of the OmpA membrane domain.";
RL J. Mol. Biol. 298:273-282(2000).
RN [47] {ECO:0007744|PDB:1G90}
RP STRUCTURE BY NMR OF 22-197, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11276254; DOI=10.1038/86214;
RA Arora A., Abildgaard F., Bushweller J.H., Tamm L.K.;
RT "Structure of outer membrane protein A transmembrane domain by NMR
RT spectroscopy.";
RL Nat. Struct. Biol. 8:334-338(2001).
RN [48] {ECO:0007744|PDB:2GE4}
RP STRUCTURE BY NMR OF 22-197, AND SUBCELLULAR LOCATION.
RX PubMed=16719475; DOI=10.1021/ja0608343;
RA Cierpicki T., Liang B., Tamm L.K., Bushweller J.H.;
RT "Increasing the accuracy of solution NMR structures of membrane proteins by
RT application of residual dipolar couplings. High-resolution structure of
RT outer membrane protein A.";
RL J. Am. Chem. Soc. 128:6947-6951(2006).
RN [49] {ECO:0007744|PDB:2JMM}
RP STRUCTURE BY NMR OF 23-197.
RX PubMed=17260943; DOI=10.1021/bi061265e;
RA Johansson M.U., Alioth S., Hu K., Walser R., Koebnik R., Pervushin K.;
RT "A minimal transmembrane beta-barrel platform protein studied by nuclear
RT magnetic resonance.";
RL Biochemistry 46:1128-1140(2007).
RN [50] {ECO:0007744|PDB:2MQE}
RP STRUCTURE BY NMR OF 201-346, SUBUNIT, DOMAIN, DISULFIDE BOND, AND
RP PEPTIDOGLYCAN-BINDING.
RC STRAIN=K12;
RX PubMed=25135663; DOI=10.1016/j.bbamem.2014.08.008;
RA Ishida H., Garcia-Herrero A., Vogel H.J.;
RT "The periplasmic domain of Escherichia coli outer membrane protein A can
RT undergo a localized temperature dependent structural transition.";
RL Biochim. Biophys. Acta 1838:3014-3024(2014).
RN [51]
RP MASS SPECTROMETRY.
RX PubMed=10757971; DOI=10.1021/bi000150m;
RA le Coutre J., Whitelegge J.P., Gross A., Turk E., Wright E.M., Kaback H.R.,
RA Faull K.F.;
RT "Proteomics on full-length membrane proteins using mass spectrometry.";
RL Biochemistry 39:4237-4242(2000).
CC -!- FUNCTION: With TolR probably plays a role in maintaining the position
CC of the peptidoglycan cell wall in the periplasm (Probable). Plays a
CC role in resistance to environmental stress, and a role in outer
CC membrane functionality and cell shape (PubMed:11906175, PubMed:361695).
CC Non-covalently binds peptidoglycan (PubMed:25135663) (Probable). Acts
CC as a porin with low permeability that allows slow penetration of small
CC solutes (PubMed:1370823, PubMed:20004640, PubMed:21069910). A very
CC abundant protein, there can be up to 210,000 OmpA molecules per cell
CC (PubMed:24766808). Reconstitution in unilamellar lipid vesicles shows
CC only about 3% of the protein is in an open conformation, which allows
CC diffusion of L-arabinose at a rate comparable to that of OmpF porin;
CC the pores interconvert very rarely (PubMed:7517935). Native and
CC reconstituted protein forms ion channels with 2 conductance states of
CC (50-80 pS) and (260-320 pS); the states are interconvertible in this
CC study. Interconversion requires refolding of the periplasmic domain
CC (PubMed:10636850). Small pores are converted into large pores by
CC increasing temperature; in this model the C-terminal periplasmic domain
CC forms 8 more beta sheets to form a larger pore (PubMed:15850404). The
CC center of the isolated beta-barrel is polar and has a central gate
CC (involving Glu-73, Lys-103, Glu-149 and Arg-159, sandwiched between
CC Tyr-29, Phe-40 and Tyr-94), with no obvious passage for water or ions
CC (PubMed:9808047) (Probable). Gating involves the Glu-73-Arg-159 salt
CC bridge; gate opening probably involves formation of alternate salt
CC bridges Glu-149-Arg-159 and Glu-73-Lys-103 (PubMed:17041590). Modeling
CC suggests that non-covalent binding of OmpA (from the outer membrane)
CC and TolR (from the inner membrane) to peptidoglycan maintains the
CC position of the cell wall in the periplasm, holding it approximately
CC equidistant from both the inner and outer membranes. Trimeric Lpp
CC controls the width of the periplasm, adjusts its tilt angle to
CC accommodate to the available space, and can compensate in part for an
CC absence of OmpA (Probable). {ECO:0000269|PubMed:10636850,
CC ECO:0000269|PubMed:11906175, ECO:0000269|PubMed:1370823,
CC ECO:0000269|PubMed:15850404, ECO:0000269|PubMed:17041590,
CC ECO:0000269|PubMed:20004640, ECO:0000269|PubMed:21069910,
CC ECO:0000269|PubMed:24766808, ECO:0000269|PubMed:25135663,
CC ECO:0000269|PubMed:361695, ECO:0000269|PubMed:7517935,
CC ECO:0000269|PubMed:9808047, ECO:0000305|PubMed:17041590,
CC ECO:0000305|PubMed:27866852, ECO:0000305|PubMed:28978443,
CC ECO:0000305|PubMed:30713026}.
CC -!- FUNCTION: Required for F plasmid cell conjugation; purified protein
CC plus lipopolysaccharide (LPS) inhibits conjugation in a concentration-
CC dependent manner. OmpA probably acts as the receptor on recipient cells
CC (PubMed:321438) (Probable). Required for the stabilization of mating
CC aggregates during F plasmid conjugative transfer, may interact with F
CC plasmid-encoded TraN, but not with TraN from plasmid R100-1
CC (PubMed:9696748, PubMed:16272376). All 4 external, surface-exposed
CC loops are required for F plasmid conjugation (PubMed:10368142).
CC {ECO:0000269|PubMed:10368142, ECO:0000269|PubMed:16272376,
CC ECO:0000269|PubMed:321438, ECO:0000269|PubMed:9696748,
CC ECO:0000305|PubMed:4604263}.
CC -!- FUNCTION: (Microbial infection) Mutants with decreased or altered
CC protein are resistant to bacteriophage TuII* (PubMed:1107069,
CC PubMed:791936). Mutants which have no or greatly reduced protein levels
CC are resistant to a number of bacteriophages, including K3, K4, K5, Ox2,
CC Ox3, Ox4, Ox5, Ml, and Ac3 (Probable) (PubMed:783129, PubMed:3902787).
CC Mutations in this protein render the bacteria partially or completely
CC susceptible to a number of bacteriophages for which is it probably the
CC receptor (PubMed:6086577, PubMed:3902787). All but the last external,
CC surface-exposed loops are required for phage K3 infection
CC (PubMed:10368142). {ECO:0000269|PubMed:10368142,
CC ECO:0000269|PubMed:1107069, ECO:0000269|PubMed:3902787,
CC ECO:0000269|PubMed:6086577, ECO:0000269|PubMed:783129,
CC ECO:0000269|PubMed:791936, ECO:0000305|PubMed:4604263}.
CC -!- FUNCTION: (Microbial infection) A mutation in this locus (called tolG)
CC renders the cell tolerant to bacteriocin JF246 but does not affect its
CC sensitivity to colicins A, C, El, E2, E3, K, Ia, or Ib
CC (PubMed:4591955). Mutations in this protein render the bacteria
CC partially or completely susceptible to colicin K or colicin L, for
CC which is it probably the receptor (PubMed:6086577).
CC {ECO:0000269|PubMed:4591955, ECO:0000269|PubMed:6086577}.
CC -!- SUBUNIT: Monomer (PubMed:1370823, PubMed:10764596, PubMed:9808047).
CC Homodimer (PubMed:16079137, PubMed:21697552, PubMed:24746938).
CC Interacts with Lpp (PubMed:3013869). About 10% of the C-terminal
CC periplasmic domain dimerizes when expressed without the N-terminal
CC domain (PubMed:25135663, PubMed:24746938). Interacts with F plasmid-
CC encoded TraN during conjugation (Probable) (PubMed:16272376).
CC {ECO:0000269|PubMed:10764596, ECO:0000269|PubMed:1370823,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:16272376,
CC ECO:0000269|PubMed:21697552, ECO:0000269|PubMed:24746938,
CC ECO:0000269|PubMed:25135663, ECO:0000269|PubMed:3013869,
CC ECO:0000269|PubMed:9808047, ECO:0000305|PubMed:9696748}.
CC -!- INTERACTION:
CC P0A910; P0C0V0: degP; NbExp=8; IntAct=EBI-371347, EBI-547165;
CC P0A910; P39099: degQ; NbExp=2; IntAct=EBI-371347, EBI-554733;
CC P0A910; P0A910: ompA; NbExp=3; IntAct=EBI-371347, EBI-371347;
CC P0A910; P69411: rcsF; NbExp=3; IntAct=EBI-371347, EBI-1114706;
CC P0A910; P10408: secA; NbExp=2; IntAct=EBI-371347, EBI-543213;
CC P0A910; P0AGA2: secY; NbExp=2; IntAct=EBI-371347, EBI-761422;
CC P0A910; P0AEU7: skp; NbExp=6; IntAct=EBI-371347, EBI-548242;
CC P0A910; P0A850: tig; NbExp=3; IntAct=EBI-371347, EBI-544862;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00842, ECO:0000269|PubMed:10636850,
CC ECO:0000269|PubMed:10947984, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:21778229, ECO:0000269|PubMed:7813480,
CC ECO:0000269|PubMed:791936, ECO:0000305|PubMed:9808047}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00842,
CC ECO:0000269|PubMed:10764596, ECO:0000269|PubMed:11276254,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:16719475,
CC ECO:0000269|PubMed:21778229, ECO:0000269|PubMed:7813480,
CC ECO:0000269|PubMed:9808047, ECO:0000305|PubMed:10636850}. Note=The 8
CC beta strands are tilted by about 45 degrees relative to the membrane
CC normal (PubMed:9808047, PubMed:10764596, PubMed:11276254,
CC PubMed:16719475). Evenly distributed on the outer membrane
CC (PubMed:10947984). {ECO:0000269|PubMed:10764596,
CC ECO:0000269|PubMed:10947984, ECO:0000269|PubMed:11276254,
CC ECO:0000269|PubMed:16719475, ECO:0000269|PubMed:9808047}.
CC -!- DOMAIN: The N-terminus transmembrane region forms low conductance pores
CC (50-80 pS); larger conductance pores (260-320 pS) are formed by the
CC whole protein. Refolding of the periplasmic domain may be required to
CC make the large conductance pores (PubMed:10636850). The structure of
CC the whole protein is controversial; the periplasmic domain may or may
CC not be inserted into the cell outer membrane to form a larger pore. The
CC protein with a narrow 8 sheet beta-barrel and a periplasmic domain may
CC be an intermediate in formation of the larger pore (Probable). The
CC disulfide bond is necessary for formation of the larger pore;
CC disulfide-bonded protein inserts into the membrane without reduction
CC (PubMed:2211627, PubMed:21069910). The isolated C-terminal periplasmic
CC domain binds peptidoglycan (PubMed:25135663, PubMed:27866852). A region
CC in the isolated periplasmic domain bulges from the rest of the protein
CC (resides 302-328) and is stabilized by the disulfide bond
CC (PubMed:25135663). {ECO:0000269|PubMed:10636850,
CC ECO:0000269|PubMed:21069910, ECO:0000269|PubMed:2211627,
CC ECO:0000269|PubMed:25135663, ECO:0000269|PubMed:27866852,
CC ECO:0000305|PubMed:10636850, ECO:0000305|PubMed:15850404,
CC ECO:0000305|PubMed:21069910}.
CC -!- PTM: Hydroxybutyrylation on Ser-184 and/or Ser-188 can add up to 10 R-
CC 3-hydroxybutyrate residues; it is not clear if one or both residues are
CC modified in vivo. Hydrophobic residues adjacent to the modified Ser
CC residues (i.e. Leu-183, Leu-185 and Val-187) are important for
CC hydroxylation. Hydroxybutyrylation occurs in the cytoplasm
CC (PubMed:17659252). Hydroxybutyrylation is required for stable pore
CC formation, unmodified protein may not be able to insert into the outer
CC membrane (PubMed:20004640). Further hydroxybutyrylation occurs in the
CC C-terminal fragment (residues 285-346); this modification probably
CC occurs in the periplasm (PubMed:21069910).
CC {ECO:0000269|PubMed:17659252, ECO:0000269|PubMed:20004640,
CC ECO:0000269|PubMed:21069910}.
CC -!- PTM: OmpA is degraded by human neutrophil elastase (ELANE) in vitro;
CC this coincides with bacterial death. Mice with a homozygous knockout of
CC ELANE are more easily killed by wild-type E.coli but not by E.coli with
CC an ompA deletion; this experiment was certainly not performed with
CC E.coli strain K12 which is no longer virulent.
CC {ECO:0000269|PubMed:10947984, ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=35177; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10757971};
CC -!- DISRUPTION PHENOTYPE: Double lpp-ompA mutants are spherical and only
CC grow in the presence of electrolytes such as 30 mM Mg(2+), and are
CC sensitive to hydrophobic antibiotics and detergents. The peptidoglycan
CC layer is no longer attached to the cell outer membrane which undergoes
CC abundant blebbing (PubMed:361695). Decreased efficiency of bacterial
CC conjugation of the F plasmid (PubMed:9696748). Deletions grow poorly on
CC SDS, cholate, at pH 3.8 or at 5 M NaCl (PubMed:11906175). Grows very
CC slowly in the absence of NaCl, wild-type growth in 1% NaCl
CC (PubMed:17041590). E.coli is no longer killed by human neutrophil
CC elastase (ELANE) in vitro (PubMed:10947984).
CC {ECO:0000269|PubMed:10947984, ECO:0000269|PubMed:11906175,
CC ECO:0000269|PubMed:17041590, ECO:0000269|PubMed:361695,
CC ECO:0000269|PubMed:9696748}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC OmpA family. {ECO:0000255|HAMAP-Rule:MF_00842}.
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DR EMBL; V00307; CAA23588.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74043.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35715.1; -; Genomic_DNA.
DR PIR; A93707; MMECA.
DR RefSeq; NP_415477.1; NC_000913.3.
DR RefSeq; WP_000750416.1; NZ_SSZK01000002.1.
DR PDB; 1BXW; X-ray; 2.50 A; A=21-192.
DR PDB; 1G90; NMR; -; A=22-197.
DR PDB; 1QJP; X-ray; 1.65 A; A=22-192.
DR PDB; 2GE4; NMR; -; A=22-197.
DR PDB; 2JMM; NMR; -; A=23-197.
DR PDB; 2MQE; NMR; -; A=201-346.
DR PDB; 3JBU; EM; 3.64 A; z=1-24.
DR PDB; 5M2Q; X-ray; 1.70 A; A/B=1-22.
DR PDB; 6ITC; EM; 3.45 A; B=2-26.
DR PDB; 6LYR; X-ray; 3.28 A; P=180-188.
DR PDBsum; 1BXW; -.
DR PDBsum; 1G90; -.
DR PDBsum; 1QJP; -.
DR PDBsum; 2GE4; -.
DR PDBsum; 2JMM; -.
DR PDBsum; 2MQE; -.
DR PDBsum; 3JBU; -.
DR PDBsum; 5M2Q; -.
DR PDBsum; 6ITC; -.
DR PDBsum; 6LYR; -.
DR AlphaFoldDB; P0A910; -.
DR BMRB; P0A910; -.
DR SMR; P0A910; -.
DR BioGRID; 4260032; 1011.
DR BioGRID; 849945; 1.
DR DIP; DIP-31879N; -.
DR IntAct; P0A910; 18.
DR MINT; P0A910; -.
DR STRING; 511145.b0957; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR TCDB; 1.B.6.1.1; the ompa-ompf porin (oop) family.
DR CarbonylDB; P0A910; -.
DR SWISS-2DPAGE; P0A910; -.
DR jPOST; P0A910; -.
DR PaxDb; P0A910; -.
DR PRIDE; P0A910; -.
DR EnsemblBacteria; AAC74043; AAC74043; b0957.
DR EnsemblBacteria; BAA35715; BAA35715; BAA35715.
DR GeneID; 945571; -.
DR KEGG; ecj:JW0940; -.
DR KEGG; eco:b0957; -.
DR PATRIC; fig|1411691.4.peg.1317; -.
DR EchoBASE; EB0663; -.
DR eggNOG; COG2885; Bacteria.
DR eggNOG; COG3637; Bacteria.
DR HOGENOM; CLU_031536_0_0_6; -.
DR InParanoid; P0A910; -.
DR OMA; HDTGFYG; -.
DR PhylomeDB; P0A910; -.
DR BioCyc; EcoCyc:EG10669-MON; -.
DR EvolutionaryTrace; P0A910; -.
DR PRO; PR:P0A910; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoliWiki.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0019867; C:outer membrane; IDA:EcoliWiki.
DR GO; GO:0106234; C:outer membrane protein complex; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015075; F:ion transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015288; F:porin activity; IDA:EcoliWiki.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0009597; P:detection of virus; IMP:EcoliWiki.
DR GO; GO:0006811; P:ion transport; IDA:EcoliWiki.
DR GO; GO:0046718; P:viral entry into host cell; IMP:EcoliWiki.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR HAMAP; MF_00842; OmpA; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR002368; OmpA.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR000498; OmpA-like_TM_dom.
DR Pfam; PF00691; OmpA; 1.
DR Pfam; PF01389; OmpA_membrane; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR PRINTS; PR01022; OUTRMMBRANEA.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Conjugation; Direct protein sequencing;
KW Disulfide bond; Host-virus interaction; Hydroxylation; Ion transport;
KW Membrane; Porin; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7001461,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9629924,
FT ECO:0000269|Ref.8"
FT CHAIN 22..346
FT /note="Outer membrane protein A"
FT /id="PRO_0000020094"
FT TOPO_DOM 22..26
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TRANSMEM 27..37
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TOPO_DOM 38..54
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TRANSMEM 55..66
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TOPO_DOM 67..69
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TRANSMEM 70..78
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TOPO_DOM 79..95
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TRANSMEM 96..107
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TOPO_DOM 108..111
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TRANSMEM 112..120
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:9808047,
FT ECO:0000305|PubMed:11276254"
FT TOPO_DOM 121..141
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:9808047,
FT ECO:0000305|PubMed:11276254"
FT TRANSMEM 142..151
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:9808047,
FT ECO:0000305|PubMed:11276254"
FT TOPO_DOM 152..155
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TRANSMEM 156..164
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TOPO_DOM 165..181
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:9808047,
FT ECO:0000305|PubMed:11276254"
FT TRANSMEM 182..191
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:11276254,
FT ECO:0000269|PubMed:9808047"
FT TOPO_DOM 192..346
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11276254,
FT ECO:0000305|PubMed:9808047"
FT REPEAT 201..202
FT /note="1"
FT REPEAT 203..204
FT /note="2"
FT REPEAT 205..206
FT /note="3"
FT REPEAT 207..208
FT /note="4"
FT DOMAIN 210..338
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
FT REGION 197..208
FT /note="Hinge-like"
FT REGION 201..208
FT /note="4 X 2 AA tandem repeats of A-P"
FT REGION 209..297
FT /note="Required for dimerization"
FT /evidence="ECO:0000269|PubMed:24746938"
FT SITE 73
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000269|PubMed:17041590"
FT SITE 159
FT /note="Part of salt bridge gating mechanism"
FT /evidence="ECO:0000269|PubMed:17041590"
FT MOD_RES 184
FT /note="O3-poly(beta-hydroxybutyryl)serine"
FT /evidence="ECO:0000269|PubMed:17659252"
FT MOD_RES 188
FT /note="O3-poly(beta-hydroxybutyryl)serine"
FT /evidence="ECO:0000269|PubMed:17659252"
FT DISULFID 311..323
FT /evidence="ECO:0000269|PubMed:25135663,
FT ECO:0000305|PubMed:21069910, ECO:0000305|PubMed:2211627"
FT VARIANT 114
FT /note="I -> V (in strain: K1 / E44)"
FT /evidence="ECO:0000269|PubMed:11906175"
FT MUTAGEN 45
FT /note="I->N: Becomes sensitive to phages K3, K4, K5, K3h1,
FT AC3, Ox3, TuII*-24, TuII*-26, partially sensitive to phages
FT TuII*-6, TuII*-60, M1."
FT /evidence="ECO:0000269|PubMed:3902787"
FT MUTAGEN 49
FT /note="G->V: Becomes sensitive to phages K3, K4, K5, K3h1,
FT TuII*-24, TuII*-26, M1, Ox2h5, Ox2h20, partially sensitive
FT to phages TuII*-46, TuII*-24, TuII*-6, AC3, Ox3."
FT /evidence="ECO:0000269|PubMed:3902787"
FT MUTAGEN 73..103
FT /note="EMGYDWLGRMPYKGSVENGAYKAQGVQLTAK->CMGYDWLGRMPYKGSVENG
FT AYKAQGVQLTAC: Nearly normal growth in absence of NaCl,
FT reducing agent (0.05% beta-mercaptoethanol) has no effect."
FT /evidence="ECO:0000269|PubMed:17041590"
FT MUTAGEN 73
FT /note="E->C: Modifies gate residues, no activity in
FT oxidizing conditions, in reducing conditions activity
FT channel opens frequently, probably forms a disulfide cross-
FT link in channel, grows very poorly in the absence of NaCl,
FT reducing agent (0.05% beta-mercaptoethanol) improves
FT growth; when associated with C-159."
FT /evidence="ECO:0000269|PubMed:17041590"
FT MUTAGEN 73
FT /note="E->Q: Higher channel activity; channel is open
FT longer and more often than wild-type, conductance does not
FT change."
FT /evidence="ECO:0000269|PubMed:17041590"
FT MUTAGEN 86
FT /note="G->D: Becomes sensitive to phages K3, K4, K3h1, M1,
FT partially sensitive to phages TuII*-6, TuII*-24, K5 Ac3,
FT Ox3, TuII-26, Ox4."
FT /evidence="ECO:0000269|PubMed:3902787,
FT ECO:0000269|PubMed:6086577"
FT MUTAGEN 86
FT /note="G->R: Becomes sensitive to phages K3h1, partially
FT sensitive to phages K4, K5, M1. Increased resistance to
FT colicin K."
FT /evidence="ECO:0000269|PubMed:6086577"
FT MUTAGEN 89
FT /note="E->G: Becomes partially sensitive to phages K3h1,
FT M1. Increased resistance to colicin K."
FT /evidence="ECO:0000269|PubMed:6086577"
FT MUTAGEN 89
FT /note="E->K: Becomes partially sensitive to phage M1.
FT Increased resistance to colicin L."
FT /evidence="ECO:0000269|PubMed:3902787,
FT ECO:0000269|PubMed:6086577"
FT MUTAGEN 89
FT /note="Missing: Becomes partially sensitive to phage M1."
FT /evidence="ECO:0000269|PubMed:3902787"
FT MUTAGEN 91
FT /note="G->C: Becomes sensitive to phages K3, K4, K5, K3h1,
FT TuII*-26, partially sensitive to phages TuII*-46, TuII*-24,
FT TuII*-6, M1, Ox2h5."
FT /evidence="ECO:0000269|PubMed:3902787"
FT MUTAGEN 91
FT /note="G->D: Becomes sensitive to phages K4, K5, K3h1,
FT partially sensitive to phages TuII*-6, TuII*-24, K3, M1."
FT /evidence="ECO:0000269|PubMed:3902787,
FT ECO:0000269|PubMed:6086577"
FT MUTAGEN 91
FT /note="G->R,V: Becomes partially sensitive to phages K3h1,
FT M1."
FT /evidence="ECO:0000269|PubMed:3902787,
FT ECO:0000269|PubMed:6086577"
FT MUTAGEN 103
FT /note="K->A: Decreased channel activity; channel opens less
FT time and less often than wild-type."
FT /evidence="ECO:0000269|PubMed:17041590"
FT MUTAGEN 126..127
FT /note="Missing: Becomes sensitive to phages Ox2, Ox4, Ox5.
FT Increased resistance to colicin L."
FT /evidence="ECO:0000269|PubMed:6086577"
FT MUTAGEN 128
FT /note="K->Y: Greatly improves X-ray-grade crystals."
FT /evidence="ECO:0000269|PubMed:9808047"
FT MUTAGEN 128
FT /note="K->Y: Restores resistance to SDS, high salt, acid
FT and cholate."
FT /evidence="ECO:0000269|PubMed:11906175"
FT MUTAGEN 129
FT /note="S->F: Becomes sensitive to phages K3, K4, K5, K3h1,
FT TuII*-26, Ox2, Ox4, Ox5, Ox2h5, Ox2h20, partially sensitive
FT to phages TuII*-46, M1."
FT /evidence="ECO:0000269|PubMed:3902787"
FT MUTAGEN 129
FT /note="S->P: Becomes sensitive to phages K3, K4, K5, K3h1,
FT TuII*-26, Ox2h5, Ox2h20."
FT /evidence="ECO:0000269|PubMed:3902787"
FT MUTAGEN 130
FT /note="N->I: Restores resistance to SDS, high salt, acid
FT and cholate."
FT /evidence="ECO:0000269|PubMed:11906175"
FT MUTAGEN 131
FT /note="V->D: Becomes sensitive to phage K3h1, Ox2h5,
FT Ox2h20, partially sensitive to phages Ox2, Ox4, Ox5, M1.
FT Increased resistance to colicin L."
FT /evidence="ECO:0000269|PubMed:3902787,
FT ECO:0000269|PubMed:6086577"
FT MUTAGEN 149
FT /note="E->A,Q: Wild-type channel activity."
FT /evidence="ECO:0000269|PubMed:17041590"
FT MUTAGEN 159
FT /note="R->A: Higher channel activity; channel is open
FT longer and more often than wild-type, conductance does not
FT change."
FT /evidence="ECO:0000269|PubMed:17041590"
FT MUTAGEN 159
FT /note="R->C: Modifies gate residues, no activity in
FT oxidizing conditions, in reducing conditions activity
FT channel opens frequently, probably forms a disulfide cross-
FT link in channel, grows very poorly in the absence of NaCl,
FT addition of reducing agent (0.05% beta-mercaptoethanol)
FT improves growth; when associated with C-173."
FT /evidence="ECO:0000269|PubMed:17041590"
FT MUTAGEN 175
FT /note="G->D,S: Becomes sensitive to phages TuII*-6, TuII*-
FT 24, TuII*-46, TuII-26, TuII*-60, K3, K4, K5, K3h1, Ac3,
FT Ox3, M1. Increased resistance to colicins K and L."
FT /evidence="ECO:0000269|PubMed:3902787,
FT ECO:0000269|PubMed:6086577"
FT MUTAGEN 183..188
FT /note="LSLGVS->GSLGVG: No longer hydroxybutyrated."
FT /evidence="ECO:0000269|PubMed:17659252"
FT MUTAGEN 184..187
FT /note="SLGV->GLGS: No longer hydroxybutyrated."
FT /evidence="ECO:0000269|PubMed:17659252"
FT MUTAGEN 184
FT /note="S->G: Protein is hydroxybutyrated. Reconstituted
FT pores have lower conductance and are open for less time. No
FT longer hydroxybutyrated, unable to form pores; when
FT associated with G-188."
FT /evidence="ECO:0000269|PubMed:17659252,
FT ECO:0000269|PubMed:20004640"
FT MUTAGEN 185..188
FT /note="LGVS->GGVG: No longer hydroxybutyrated."
FT /evidence="ECO:0000269|PubMed:17659252"
FT MUTAGEN 188
FT /note="S->G: Protein is hydroxybutyrated. Reconstituted
FT pores have lower conductance. No longer hydroxybutyrated,
FT unable to form pores; when associated with G-184."
FT /evidence="ECO:0000269|PubMed:17659252,
FT ECO:0000269|PubMed:20004640"
FT MUTAGEN 189
FT /note="Y->F: Protein is hydroxybutyrated."
FT /evidence="ECO:0000269|PubMed:17659252"
FT MUTAGEN 190
FT /note="R->D,N: Protein is hydroxybutyrated."
FT /evidence="ECO:0000269|PubMed:17659252"
FT MUTAGEN 213
FT /note="K->A: No longer dimerizes."
FT /evidence="ECO:0000269|PubMed:24746938"
FT MUTAGEN 248..346
FT /note="Missing: No longer dimerizes."
FT /evidence="ECO:0000269|PubMed:24746938"
FT MUTAGEN 294..346
FT /note="Missing: Still dimerizes."
FT /evidence="ECO:0000269|PubMed:24746938"
FT MUTAGEN 311
FT /note="C->G: Protein insertion into vesicles is not blocked
FT by ferricyanide."
FT /evidence="ECO:0000269|PubMed:2211627"
FT MUTAGEN 338
FT /note="K->A: Still dimerizes."
FT /evidence="ECO:0000269|PubMed:24746938"
FT HELIX 2..18
FT /evidence="ECO:0007829|PDB:6ITC"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6ITC"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:6ITC"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:1QJP"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1G90"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1G90"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2GE4"
FT STRAND 55..67
FT /evidence="ECO:0007829|PDB:1QJP"
FT STRAND 70..81
FT /evidence="ECO:0007829|PDB:1QJP"
FT STRAND 93..128
FT /evidence="ECO:0007829|PDB:1QJP"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1QJP"
FT STRAND 134..153
FT /evidence="ECO:0007829|PDB:1QJP"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:1QJP"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:1G90"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:1QJP"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:2MQE"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:2MQE"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2MQE"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:2MQE"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:2MQE"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:2MQE"
FT HELIX 267..286
FT /evidence="ECO:0007829|PDB:2MQE"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:2MQE"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:2MQE"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:2MQE"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:2MQE"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:2MQE"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:2MQE"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:2MQE"
SQ SEQUENCE 346 AA; 37201 MW; 195147734CDF8B04 CRC64;
MKKTAIAIAV ALAGFATVAQ AAPKDNTWYT GAKLGWSQYH DTGFINNNGP THENQLGAGA
FGGYQVNPYV GFEMGYDWLG RMPYKGSVEN GAYKAQGVQL TAKLGYPITD DLDIYTRLGG
MVWRADTKSN VYGKNHDTGV SPVFAGGVEY AITPEIATRL EYQWTNNIGD AHTIGTRPDN
GMLSLGVSYR FGQGEAAPVV APAPAPAPEV QTKHFTLKSD VLFNFNKATL KPEGQAALDQ
LYSQLSNLDP KDGSVVVLGY TDRIGSDAYN QGLSERRAQS VVDYLISKGI PADKISARGM
GESNPVTGNT CDNVKQRAAL IDCLAPDRRV EIEVKGIKDV VTQPQA
