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Outer membrane protein A (Outer membrane protein II*)

 OMPA_ECOLI              Reviewed;         346 AA.
P0A910; P02934;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=Outer membrane protein A;
AltName: Full=Outer membrane protein II*;
Flags: Precursor;
Name=ompA; Synonyms=con, tolG, tut; OrderedLocusNames=b0957, JW0940;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6253901; DOI=10.1093/nar/8.13.3011;
Beck E., Bremer E.;
"Nucleotide sequence of the gene ompA coding the outer membrane
protein II of Escherichia coli K-12.";
Nucleic Acids Res. 8:3011-3027(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6260961; DOI=10.1016/0022-2836(80)90193-X;
Movva N.R., Nakamura K., Inouye M.;
"Gene structure of the OmpA protein, a major surface protein of
Escherichia coli required for cell-cell interaction.";
J. Mol. Biol. 143:317-328(1980).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 22-346.
STRAIN=K12;
PubMed=7001461; DOI=10.1073/pnas.77.8.4592;
Chen R., Schmidmayr W., Kramer C., Chen-Schmeisser U., Henning U.;
"Primary structure of major outer membrane protein II (ompA protein)
of Escherichia coli K-12.";
Proc. Natl. Acad. Sci. U.S.A. 77:4592-4596(1980).
[7]
PROTEIN SEQUENCE OF 22-34.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
PROTEIN SEQUENCE OF 22-32.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J.,
Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A.,
Hochstrasser D.F.;
Submitted (SEP-1994) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 22-26.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9629924; DOI=10.1002/elps.1150190539;
Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M.,
Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
"Extraction of membrane proteins by differential solubilization for
separation using two-dimensional gel electrophoresis.";
Electrophoresis 19:837-844(1998).
[10]
MUTANTS RESISTANT TO PHAGE ENTRY.
PubMed=6086577;
Morona R., Klose M., Henning U.;
"Escherichia coli K-12 outer membrane protein (OmpA) as a
bacteriophage receptor: analysis of mutant genes expressing altered
proteins.";
J. Bacteriol. 159:570-578(1984).
[11]
MUTANTS RESISTANT TO PHAGE ENTRY.
PubMed=3902787;
Morona R., Kramer C., Henning U.;
"Bacteriophage receptor area of outer membrane protein OmpA of
Escherichia coli K-12.";
J. Bacteriol. 164:539-543(1985).
[12]
PORIN ACTIVITY.
STRAIN=K12;
PubMed=1370823;
Sugawara E., Nikaido H.;
"Pore-forming activity of OmpA protein of Escherichia coli.";
J. Biol. Chem. 267:2507-2511(1992).
[13]
SUBCELLULAR LOCATION.
PubMed=7813480; DOI=10.1111/j.1432-1033.1994.00891.x;
Kuhn A., Kiefer D., Koehne C., Zhu H.-Y., Tschantz W.R., Dalbey R.E.;
"Evidence for a loop-like insertion mechanism of pro-Omp A into the
inner membrane of Escherichia coli.";
Eur. J. Biochem. 226:891-897(1994).
[14]
TOPOLOGY.
PubMed=8106193;
Gromiha M.M., Ponnuswamy P.K.;
"Prediction of transmembrane beta-strands from hydrophobic
characteristics of proteins.";
Int. J. Pept. Protein Res. 42:420-431(1993).
[15]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[16]
TOPOLOGY.
PubMed=10368142;
Koebnik R.;
"Structural and functional roles of the surface-exposed loops of the
beta-barrel membrane protein OmpA from Escherichia coli.";
J. Bacteriol. 181:3688-3694(1999).
[17]
DIMERIZATION, AND SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
PubMed=16079137; DOI=10.1074/jbc.M506479200;
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[18]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=21778229; DOI=10.1074/jbc.M111.245696;
Fontaine F., Fuchs R.T., Storz G.;
"Membrane localization of small proteins in Escherichia coli.";
J. Biol. Chem. 286:32464-32474(2011).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-192.
PubMed=9808047; DOI=10.1038/2983;
Pautsch A., Schulz G.E.;
"Structure of the outer membrane protein A transmembrane domain.";
Nat. Struct. Biol. 5:1013-1017(1998).
[20]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
PubMed=10764596; DOI=10.1006/jmbi.2000.3671;
Pautsch A., Schulz G.E.;
"High-resolution structure of the OmpA membrane domain.";
J. Mol. Biol. 298:273-282(2000).
[21]
STRUCTURE BY NMR OF 22-197.
PubMed=11276254; DOI=10.1038/86214;
Arora A., Abildgaard F., Bushweller J.H., Tamm L.K.;
"Structure of outer membrane protein A transmembrane domain by NMR
spectroscopy.";
Nat. Struct. Biol. 8:334-338(2001).
[22]
MASS SPECTROMETRY.
PubMed=10757971; DOI=10.1021/bi000150m;
le Coutre J., Whitelegge J.P., Gross A., Turk E., Wright E.M.,
Kaback H.R., Faull K.F.;
"Proteomics on full-length membrane proteins using mass
spectrometry.";
Biochemistry 39:4237-4242(2000).
-!- FUNCTION: Required for the action of colicins K and L and for the
stabilization of mating aggregates in conjugation. Serves as a
receptor for a number of T-even like phages. Also acts as a porin
with low permeability that allows slow penetration of small
solutes.
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-371347, EBI-371347;
P0C0V0:degP; NbExp=9; IntAct=EBI-371347, EBI-547165;
P39099:degQ; NbExp=2; IntAct=EBI-371347, EBI-554733;
P69411:rcsF; NbExp=3; IntAct=EBI-371347, EBI-1114706;
P10408:secA; NbExp=2; IntAct=EBI-371347, EBI-543213;
P0AGA2:secY; NbExp=2; IntAct=EBI-371347, EBI-761422;
P0AEU7:skp; NbExp=6; IntAct=EBI-371347, EBI-548242;
P0A850:tig; NbExp=3; IntAct=EBI-371347, EBI-544862;
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229,
ECO:0000269|PubMed:7813480}; Multi-pass membrane protein
{ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229,
ECO:0000269|PubMed:7813480}.
-!- MASS SPECTROMETRY: Mass=35177; Method=Electrospray; Range=22-346;
Evidence={ECO:0000269|PubMed:10757971};
-!- SIMILARITY: Belongs to the OmpA family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; V00307; CAA23588.1; -; Genomic_DNA.
EMBL; U00096; AAC74043.1; -; Genomic_DNA.
EMBL; AP009048; BAA35715.1; -; Genomic_DNA.
PIR; A93707; MMECA.
RefSeq; NP_415477.1; NC_000913.3.
RefSeq; WP_000750416.1; NZ_LN832404.1.
PDB; 1BXW; X-ray; 2.50 A; A=21-192.
PDB; 1G90; NMR; -; A=22-197.
PDB; 1QJP; X-ray; 1.65 A; A=22-192.
PDB; 2GE4; NMR; -; A=22-197.
PDB; 2JMM; NMR; -; A=23-197.
PDB; 3JBU; EM; 3.64 A; z=1-24.
PDB; 3NB3; EM; -; A/B/C=1-346.
PDB; 5M2Q; X-ray; 1.70 A; A/B=1-22.
PDBsum; 1BXW; -.
PDBsum; 1G90; -.
PDBsum; 1QJP; -.
PDBsum; 2GE4; -.
PDBsum; 2JMM; -.
PDBsum; 3JBU; -.
PDBsum; 3NB3; -.
PDBsum; 5M2Q; -.
ProteinModelPortal; P0A910; -.
SMR; P0A910; -.
BioGrid; 4260032; 1011.
BioGrid; 849945; 1.
DIP; DIP-31879N; -.
IntAct; P0A910; 18.
MINT; MINT-1308131; -.
STRING; 316385.ECDH10B_1027; -.
DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
TCDB; 1.B.6.1.1; the ompa-ompf porin (oop) family.
SWISS-2DPAGE; P0A910; -.
PaxDb; P0A910; -.
PRIDE; P0A910; -.
EnsemblBacteria; AAC74043; AAC74043; b0957.
EnsemblBacteria; BAA35715; BAA35715; BAA35715.
GeneID; 945571; -.
KEGG; ecj:JW0940; -.
KEGG; eco:b0957; -.
PATRIC; fig|1411691.4.peg.1317; -.
EchoBASE; EB0663; -.
EcoGene; EG10669; ompA.
eggNOG; ENOG4105UYK; Bacteria.
eggNOG; COG2885; LUCA.
HOGENOM; HOG000274199; -.
InParanoid; P0A910; -.
KO; K03286; -.
BioCyc; EcoCyc:EG10669-MONOMER; -.
EvolutionaryTrace; P0A910; -.
PRO; PR:P0A910; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009279; C:cell outer membrane; IDA:EcoliWiki.
GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
GO; GO:0016020; C:membrane; IDA:EcoliWiki.
GO; GO:0019867; C:outer membrane; IDA:EcoliWiki.
GO; GO:0046930; C:pore complex; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0015288; F:porin activity; IDA:EcoCyc.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
GO; GO:0000746; P:conjugation; IMP:EcoliWiki.
GO; GO:0009597; P:detection of virus; IMP:EcoliWiki.
GO; GO:0034220; P:ion transmembrane transport; IDA:EcoCyc.
GO; GO:0006811; P:ion transport; IDA:EcoliWiki.
GO; GO:0006810; P:transport; IDA:EcoliWiki.
GO; GO:0046718; P:viral entry into host cell; IMP:EcoliWiki.
CDD; cd07185; OmpA_C-like; 1.
Gene3D; 2.40.160.20; -; 1.
Gene3D; 3.30.1330.60; -; 1.
InterPro; IPR011250; OMP/PagP_b-brl.
InterPro; IPR006664; OMP_bac.
InterPro; IPR002368; OmpA.
InterPro; IPR006665; OmpA-like.
InterPro; IPR006690; OMPA-like_CS.
InterPro; IPR036737; OmpA-like_sf.
InterPro; IPR000498; OmpA-like_TM_dom.
Pfam; PF00691; OmpA; 1.
Pfam; PF01389; OmpA_membrane; 1.
PRINTS; PR01021; OMPADOMAIN.
PRINTS; PR01022; OUTRMMBRANEA.
SUPFAM; SSF103088; SSF103088; 1.
SUPFAM; SSF56925; SSF56925; 1.
PROSITE; PS01068; OMPA_1; 1.
PROSITE; PS51123; OMPA_2; 1.
1: Evidence at protein level;
3D-structure; Cell outer membrane; Complete proteome; Conjugation;
Direct protein sequencing; Disulfide bond; Ion transport; Membrane;
Porin; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane beta strand; Transport.
SIGNAL 1 21 {ECO:0000269|PubMed:7001461,
ECO:0000269|PubMed:9298646,
ECO:0000269|PubMed:9629924,
ECO:0000269|Ref.8}.
CHAIN 22 346 Outer membrane protein A.
/FTId=PRO_0000020094.
TOPO_DOM 22 26 Periplasmic.
TRANSMEM 27 37 Beta stranded.
TOPO_DOM 38 54 Extracellular.
TRANSMEM 55 66 Beta stranded.
TOPO_DOM 67 69 Periplasmic.
TRANSMEM 70 78 Beta stranded.
TOPO_DOM 79 95 Extracellular.
TRANSMEM 96 107 Beta stranded.
TOPO_DOM 108 111 Periplasmic.
TRANSMEM 112 124 Beta stranded.
TOPO_DOM 125 137 Extracellular.
TRANSMEM 138 151 Beta stranded.
TOPO_DOM 152 155 Periplasmic.
TRANSMEM 156 163 Beta stranded.
TOPO_DOM 164 181 Extracellular.
TRANSMEM 182 190 Beta stranded.
TOPO_DOM 191 346 Periplasmic.
REPEAT 201 202 1.
REPEAT 203 204 2.
REPEAT 205 206 3.
REPEAT 207 208 4.
DOMAIN 210 338 OmpA-like. {ECO:0000255|PROSITE-
ProRule:PRU00473}.
REGION 197 208 Hinge-like.
REGION 201 208 4 X 2 AA tandem repeats of A-P.
DISULFID 311 323
STRAND 27 37 {ECO:0000244|PDB:1QJP}.
STRAND 41 43 {ECO:0000244|PDB:1G90}.
STRAND 46 48 {ECO:0000244|PDB:1G90}.
STRAND 50 53 {ECO:0000244|PDB:2GE4}.
STRAND 55 67 {ECO:0000244|PDB:1QJP}.
STRAND 70 81 {ECO:0000244|PDB:1QJP}.
STRAND 93 128 {ECO:0000244|PDB:1QJP}.
STRAND 130 132 {ECO:0000244|PDB:1QJP}.
STRAND 134 153 {ECO:0000244|PDB:1QJP}.
STRAND 156 165 {ECO:0000244|PDB:1QJP}.
TURN 172 175 {ECO:0000244|PDB:1G90}.
STRAND 182 190 {ECO:0000244|PDB:1QJP}.
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


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