OMPC_ECOL6
ID OMPC_ECOL6 Reviewed; 375 AA.
AC Q8CVW1;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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; OrderedLocusNames=c2758;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF 173-GLN--ARG-196 AND
RP 229-TRP--THR-239.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 22-375, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=22053181; DOI=10.1371/journal.pone.0025825;
RA Lou H., Chen M., Black S.S., Bushell S.R., Ceccarelli M., Mach T., Beis K.,
RA Low A.S., Bamford V.A., Booth I.R., Bayley H., Naismith J.H.;
RT "Altered antibiotic transport in OmpC mutants isolated from a series of
RT clinical strains of multi-drug resistant E. coli.";
RL PLoS ONE 6:E25825-E25825(2011).
CC -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC across the outer membrane, including some antibiotics. Variation of the
CC residues in the constriction zone modifies the transverse electric
CC field in the zone, altering antibiotic resistance.
CC {ECO:0000269|PubMed:22053181}.
CC -!- FUNCTION: (Microbial infection) Is not susceptible to CdiA-EC536-
CC mediated toxicity, which uses OmpC-OmpF heterotrimers of some strains
CC as its outer membrane receptor. Mutagenesis of extracellular loops L4
CC or L5 of this protein confers susceptibility to the toxin.
CC {ECO:0000269|PubMed:27723824}.
CC -!- SUBUNIT: Homotrimer (PubMed:22053181). Forms mixed heterotrimers with
CC OmpF; other mixed heterotrimers are also probable (Probable). The
CC N- and C-termini are two parts of the same strand. Extracellular loop 3
CC folds back into the lumen of the barrel forming a constriction zone
CC that controls the pore size, while the trimer interface is formed by
CC the packing of hydrophobic residues on the outer edges of beta strands
CC 1 to 5 and further stabilized by extracellular loop 2 which reaches
CC into the neighboring monomer (PubMed:22053181).
CC {ECO:0000269|PubMed:22053181, ECO:0000305|PubMed:27723824}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:22053181,
CC ECO:0000305|PubMed:27723824}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22053181}.
CC -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR EMBL; AE014075; AAN81212.1; -; Genomic_DNA.
DR RefSeq; WP_000865543.1; NC_004431.1.
DR PDB; 2XE1; X-ray; 2.50 A; A=22-375.
DR PDBsum; 2XE1; -.
DR AlphaFoldDB; Q8CVW1; -.
DR SMR; Q8CVW1; -.
DR STRING; 199310.c2758; -.
DR EnsemblBacteria; AAN81212; AAN81212; c2758.
DR KEGG; ecc:c2758; -.
DR eggNOG; COG3203; Bacteria.
DR HOGENOM; CLU_058202_0_0_6; -.
DR OMA; DNKENSW; -.
DR BioCyc; ECOL199310:C2758-MON; -.
DR EvolutionaryTrace; Q8CVW1; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0034220; P:ion transmembrane transport; IEA:InterPro.
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; Ion transport; Membrane; Porin; Signal;
KW Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..375
FT /note="Outer membrane porin C"
FT /id="PRO_0000025231"
FT TRANSMEM 22..27
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 28..29
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 30..44
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 45..50
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 51..66
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 67..70
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 71..82
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 83..91
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 92..103
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 104..105
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 106..113
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 114..146
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 147..156
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 157..163
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 164..172
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 173..201
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22053181,
FT ECO:0000269|PubMed:27723824"
FT TRANSMEM 202..212
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 213..215
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 216..226
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 227..241
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22053181,
FT ECO:0000269|PubMed:27723824"
FT TRANSMEM 242..254
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 255..256
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 257..267
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 268..279
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 280..292
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 293..294
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 295..309
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 310..320
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 321..335
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 336..338
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 339..348
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TOPO_DOM 349..364
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22053181"
FT TRANSMEM 365..375
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:22053181"
FT MUTAGEN 173..196
FT /note="QNGSVSGENDPDFTGHGITNNGRK->KNGSVSGEGMTNNGRD: Becomes
FT susceptible to CdiA-EC536; replaces extracellular loop 4
FT with that of OmpC from strain F11."
FT /evidence="ECO:0000269|PubMed:27723824"
FT MUTAGEN 229..239
FT /note="WDQNNTGLIGT->DAQNTAAYIGN: Becomes susceptible to
FT CdiA-EC536; replaces extracellular loop 5 with that of OmpC
FT from strain EC536."
FT /evidence="ECO:0000269|PubMed:27723824"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 30..46
FT /evidence="ECO:0007829|PDB:2XE1"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 68..85
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:2XE1"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2XE1"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:2XE1"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:2XE1"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2XE1"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 203..213
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 216..226
FT /evidence="ECO:0007829|PDB:2XE1"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 241..254
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 257..268
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 295..309
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 316..336
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:2XE1"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:2XE1"
FT STRAND 366..375
FT /evidence="ECO:0007829|PDB:2XE1"
SQ SEQUENCE 375 AA; 41225 MW; 8B83426194FDC235 CRC64;
MKVKVLSLLV PALLVAGAAN AAEVYNKDGN KLDLYGKVDG LHYFSDDKSV DGDQTYMRLG
FKGETQVTDQ LTGYGQWEYQ IQGNAPESEN NSWTRVAFAG LKFQDIGSFD YGRNYGVVYD
VTSWTDVLPE FGGDTYGSDN FMQQRGNGFA TYRNTDFFGL VDGLNFAVQY QGQNGSVSGE
NDPDFTGHGI TNNGRKALRQ NGDGVGGSIT YDYEGFGVGA AVSSSKRTWD QNNTGLIGTG
DRAETYTGGL KYDANNIYLA AQYTQTYNAT RVGSLGWANK AQNFEAVAQY QFDFGLRPSV
AYLQSKGKNL GVVAGRNYDD EDILKYVDVG ATYYFNKNMS TYVDYKINLL DDNQFTRAAG
INTDDIVALG LVYQF
