OMPC_ECOL5
ID OMPC_ECOL5 Reviewed; 375 AA.
AC P0DQH0; A0A454A607;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 25-MAY-2022, entry version 12.
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=ECP_2258;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
RN [2]
RP FUNCTION (MICROBIAL INFECTION), AND SUBUNIT.
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).
CC -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC across the outer membrane. {ECO:0000250|UniProtKB:Q8CVW1}.
CC -!- FUNCTION: (Microbial infection) Supports colicin E5 entry in the
CC absence of its major receptor OmpF. {ECO:0000269|PubMed:27723824}.
CC -!- FUNCTION: (Microbial infection) A mixed OmpC-OmpF heterotrimer is the
CC outer membrane receptor for toxin CdiA-EC536.
CC {ECO:0000269|PubMed:27723824}.
CC -!- SUBUNIT: Homotrimer (Probable). Forms mixed heterotrimers with OmpF;
CC other mixed heterotrimers are also probable (PubMed:27723824).
CC {ECO:0000269|PubMed:27723824, ECO:0000305|PubMed:27723824}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:27723824}; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR EMBL; CP000247; ABG70254.1; -; Genomic_DNA.
DR RefSeq; WP_000865542.1; NC_008253.1.
DR AlphaFoldDB; P0DQH0; -.
DR SMR; P0DQH0; -.
DR STRING; 362663.ECP_2258; -.
DR EnsemblBacteria; ABG70254; ABG70254; ECP_2258.
DR KEGG; ecp:ECP_2258; -.
DR OMA; DNKENSW; -.
DR Proteomes; UP000009182; 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 Cell outer membrane; Ion transport; Membrane; Porin; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..375
FT /note="Outer membrane porin C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000446878"
FT TOPO_DOM 22..33
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..42
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 43..53
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..63
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 64..73
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..84
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 85..91
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 92..101
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 102..106
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 107..115
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 116..141
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..154
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 155..163
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 164..171
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 172..204
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27723824"
FT TRANSMEM 205..211
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 212..215
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..223
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 224..245
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27723824"
FT TRANSMEM 246..252
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 253..256
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 257..264
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 265..273
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..290
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 291..295
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..303
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 304..326
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..334
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 335..338
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 339..346
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 347..366
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..374
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P06996"
FT TOPO_DOM 375
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 41233 MW; 31BC0C01CF061DD9 CRC64;
MKVKVLSLLV PALLVAGAAN AAEVYNKDGN KLDLYGKVDG LHYFSDDKSV DGDQTYMRLG
FKGETQVTDQ LTGYGQWEYQ IQGNAPESEN NSWTRVAFAG LKFQDIGSFD YGRNYGVVYD
VTSWTDVLPE FGGDTYGSDN FMQQRGNGFA TYRNTDFFGL VDGLNFAVQY QGQNGSVSGE
NDPDFTGHGI TNNGRKALRQ NGDGVGGSIT YDYEGFGVGA AVSSSKRTDA QNTAAYIGNG
DRAETYTGGL KYDANNIYLA AQYTQTYNAT RVGSLGWANK AQNFEAVAQY QFDFGLRPSV
AYLQSKGKNL GTIGTRNYDD EDILKYVDVG ATYYFNKNMS TYVDYKINLL DDNQFTRDAG
INTDNIVALG LVYQF
