OMPC_ECOLI
ID OMPC_ECOLI Reviewed; 367 AA.
AC P06996;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Outer membrane porin C;
DE AltName: Full=Outer membrane protein 1B;
DE AltName: Full=Outer membrane protein C;
DE AltName: Full=Porin OmpC;
DE Flags: Precursor;
GN Name=ompC; Synonyms=meoA, par; OrderedLocusNames=b2215, JW2203;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6304064; DOI=10.1016/s0021-9258(18)32313-5;
RA Mizuno T., Chou M.-Y., Inouye M.;
RT "A comparative study on the genes for three porins of the Escherichia coli
RT outer membrane. DNA sequence of the osmoregulated ompC gene.";
RL J. Biol. Chem. 258:6932-6940(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(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 [LARGE SCALE GENOMIC DNA] OF 218-367.
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22, AND PROTEIN SEQUENCE OF 22-40.
RX PubMed=6297988; DOI=10.1016/0014-5793(83)80364-0;
RA Mizuno T., Chou M.-Y., Inouye M.;
RT "DNA sequence of the promoter region of the ompC gene and the amino acid
RT sequence of the signal peptide of pro-OmpC protein of Escherichia coli.";
RL FEBS Lett. 151:159-164(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-57.
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 22-30.
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 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 INDUCTION BY HIGH 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 HIGH 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 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 [14]
RP INDUCTION.
RC STRAIN=K12 / MC4100;
RX PubMed=28423182; DOI=10.1002/1873-3468.12658;
RA Hwang E., Cheong H.K., Kim S.Y., Kwon O., Blain K.Y., Choe S., Yeo K.J.,
RA Jung Y.W., Jeon Y.H., Cheong C.;
RT "Crystal structure of the EnvZ periplasmic domain with CHAPS.";
RL FEBS Lett. 591:1419-1428(2017).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-367 IN COMPLEX WITH MG(2+),
RP SUBUNIT, DOMAIN, AND TOPOLOGY.
RX PubMed=16949612; DOI=10.1016/j.jmb.2006.08.002;
RA Basle A., Rummel G., Storici P., Rosenbusch J.P., Schirmer T.;
RT "Crystal structure of osmoporin OmpC from E. coli at 2.0 A.";
RL J. Mol. Biol. 362:933-942(2006).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 22-367.
RA Baalaji S., Acharya R.K., Singh T.P., Krishnaswamy S.;
RT "Crystal structure of the membrane protein Ompc complex with antibacterial
RT lactoferrin.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC across the outer membrane.
CC -!- FUNCTION: (Microbial infection) Supports colicin E5 entry in the
CC absence of its major receptor OmpF. {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:16949612). Forms mixed
CC heterotrimers with OmpF and with PhoE; other mixed heterotrimers are
CC also probable (PubMed:2464593). {ECO:0000269|PubMed:16949612,
CC ECO:0000269|PubMed:2464593}.
CC -!- INTERACTION:
CC P06996; P0C0V0: degP; NbExp=7; IntAct=EBI-371155, EBI-547165;
CC P06996; P76506: mlaA; NbExp=4; IntAct=EBI-371155, EBI-1128511;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2464593};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16949612}.
CC -!- INDUCTION: By growth in high osmolarity conditions (high sugar or salt)
CC under control of OmpR (at protein level) (PubMed:3010044,
CC PubMed:2464593). In the presence of 0.2 M NaCl, 2.0 mM sodium cholate
CC (bile salts) decreases expression from the ompC promoter; how this is
CC mediated is unknown (PubMed:28423182). {ECO:0000269|PubMed:2464593,
CC ECO:0000269|PubMed:28423182, ECO:0000269|PubMed:3010044}.
CC -!- DOMAIN: Loop L3 (residues 116-133) extends along the inner side of the
CC beta barrel wall and may constrict the pore mid-length.
CC {ECO:0000269|PubMed:16949612}.
CC -!- DISRUPTION PHENOTYPE: Deletion of both ompC and ompF confers resistance
CC to colicin E5 and to the toxic activity of CdiA-EC536.
CC {ECO:0000269|PubMed:27723824}.
CC -!- MISCELLANEOUS: Binds 1 Mg(2+) per subunit; could be Ca(2+) in vivo.
CC -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR EMBL; K00541; AAA24243.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75275.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15998.1; -; Genomic_DNA.
DR EMBL; U00008; AAA16412.1; -; Genomic_DNA.
DR PIR; A20867; MMECPC.
DR RefSeq; NP_416719.1; NC_000913.3.
DR RefSeq; WP_000865568.1; NZ_SSZK01000030.1.
DR PDB; 2J1N; X-ray; 2.00 A; A/B/C=22-367.
DR PDB; 2J4U; X-ray; 2.99 A; P/Q/R/U/V/W=22-367.
DR PDB; 2ZLE; EM; 28.00 A; D=22-367.
DR PDB; 4A8D; EM; 28.00 A; M=22-366.
DR PDBsum; 2J1N; -.
DR PDBsum; 2J4U; -.
DR PDBsum; 2ZLE; -.
DR PDBsum; 4A8D; -.
DR AlphaFoldDB; P06996; -.
DR SMR; P06996; -.
DR BioGRID; 4261917; 276.
DR DIP; DIP-10397N; -.
DR IntAct; P06996; 9.
DR MINT; P06996; -.
DR STRING; 511145.b2215; -.
DR DrugBank; DB01017; Minocycline.
DR TCDB; 1.B.1.1.3; the general bacterial porin (gbp) family.
DR jPOST; P06996; -.
DR PaxDb; P06996; -.
DR PRIDE; P06996; -.
DR EnsemblBacteria; AAC75275; AAC75275; b2215.
DR EnsemblBacteria; BAA15998; BAA15998; BAA15998.
DR GeneID; 946716; -.
DR KEGG; ecj:JW2203; -.
DR KEGG; eco:b2215; -.
DR PATRIC; fig|1411691.4.peg.20; -.
DR EchoBASE; EB0664; -.
DR eggNOG; COG3203; Bacteria.
DR HOGENOM; CLU_058202_0_0_6; -.
DR InParanoid; P06996; -.
DR OMA; DNKENSW; -.
DR PhylomeDB; P06996; -.
DR BioCyc; EcoCyc:EG10670-MON; -.
DR BioCyc; MetaCyc:EG10670-MON; -.
DR EvolutionaryTrace; P06996; -.
DR PHI-base; PHI:7024; -.
DR PRO; PR:P06996; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoliWiki.
DR GO; GO:0046930; C:pore complex; TAS:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IDA:EcoCyc.
DR GO; GO:0001618; F:virus receptor activity; IDA:CACAO.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0034220; P:ion transmembrane transport; IEA:InterPro.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:CACAO.
DR Gene3D; 2.40.160.10; -; 1.
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; Magnesium; Membrane; Metal-binding; Porin;
KW Reference proteome; Signal; Stress response; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:6297988,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9629924"
FT CHAIN 22..367
FT /note="Outer membrane porin C"
FT /id="PRO_0000025230"
FT TOPO_DOM 22..33
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 34..42
FT /note="Beta stranded"
FT TOPO_DOM 43..53
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 54..63
FT /note="Beta stranded"
FT TOPO_DOM 64..73
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 74..84
FT /note="Beta stranded"
FT TOPO_DOM 85..91
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 92..101
FT /note="Beta stranded"
FT TOPO_DOM 102..106
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 107..115
FT /note="Beta stranded"
FT TOPO_DOM 116..141
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 142..154
FT /note="Beta stranded"
FT TOPO_DOM 155..163
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 164..171
FT /note="Beta stranded"
FT TOPO_DOM 172..200
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 201..207
FT /note="Beta stranded"
FT TOPO_DOM 208..211
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 212..219
FT /note="Beta stranded"
FT TOPO_DOM 220..241
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 242..248
FT /note="Beta stranded"
FT TOPO_DOM 249..252
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 253..260
FT /note="Beta stranded"
FT TOPO_DOM 261..269
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 270..286
FT /note="Beta stranded"
FT TOPO_DOM 287..291
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 292..299
FT /note="Beta stranded"
FT TOPO_DOM 300..318
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 319..326
FT /note="Beta stranded"
FT TOPO_DOM 327..330
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 331..338
FT /note="Beta stranded"
FT TOPO_DOM 339..358
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16949612"
FT TRANSMEM 359..366
FT /note="Beta stranded"
FT TOPO_DOM 367
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:16949612"
FT REGION 116..133
FT /note="Loop L3; may constrict the pore"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:2J1N"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:2J1N"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:2J1N"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 30..44
FT /evidence="ECO:0007829|PDB:2J1N"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 56..85
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:2J1N"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2J1N"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:2J1N"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:2J1N"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:2J4U"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2J1N"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 212..222
FT /evidence="ECO:0007829|PDB:2J1N"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2J4U"
FT STRAND 237..250
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 253..264
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 275..286
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 291..305
FT /evidence="ECO:0007829|PDB:2J1N"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:2J4U"
FT STRAND 312..340
FT /evidence="ECO:0007829|PDB:2J1N"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:2J1N"
FT STRAND 358..367
FT /evidence="ECO:0007829|PDB:2J1N"
SQ SEQUENCE 367 AA; 40368 MW; 6A49370CC8A1A225 CRC64;
MKVKVLSLLV PALLVAGAAN AAEVYNKDGN KLDLYGKVDG LHYFSDNKDV DGDQTYMRLG
FKGETQVTDQ LTGYGQWEYQ IQGNSAENEN NSWTRVAFAG LKFQDVGSFD YGRNYGVVYD
VTSWTDVLPE FGGDTYGSDN FMQQRGNGFA TYRNTDFFGL VDGLNFAVQY QGKNGNPSGE
GFTSGVTNNG RDALRQNGDG VGGSITYDYE GFGIGGAISS SKRTDAQNTA AYIGNGDRAE
TYTGGLKYDA NNIYLAAQYT QTYNATRVGS LGWANKAQNF EAVAQYQFDF GLRPSLAYLQ
SKGKNLGRGY DDEDILKYVD VGATYYFNKN MSTYVDYKIN LLDDNQFTRD AGINTDNIVA
LGLVYQF
