OMPG_ECOLI
ID OMPG_ECOLI Reviewed; 301 AA.
AC P76045; Q2MBF5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Outer membrane porin G;
DE AltName: Full=Outer membrane protein G;
DE Flags: Precursor;
GN Name=ompG; OrderedLocusNames=b1319, JW1312;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 22-35.
RC STRAIN=K12;
RX PubMed=9721282; DOI=10.1128/jb.180.17.4452-4459.1998;
RA Fajardo D.A., Cheung J., Ito C., Sugawara E., Nikaido H., Misra R.;
RT "Biochemistry and regulation of a novel Escherichia coli K-12 porin
RT protein, OmpG, which produces unusually large channels.";
RL J. Bacteriol. 180:4452-4459(1998).
RN [2]
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 [3]
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 [4]
RP FUNCTION IN THE REGULATION OF THE RCS SYSTEM.
RX PubMed=11758943; DOI=10.1271/bbb.65.2364;
RA Chen M.H., Takeda S., Yamada H., Ishii Y., Yamashino T., Mizuno T.;
RT "Characterization of the RcsC->YojN->RcsB phosphorelay signaling pathway
RT involved in capsular synthesis in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 65:2364-2367(2001).
CC -!- FUNCTION: Forms channels functionally larger than those of classical
CC porins. {ECO:0000269|PubMed:11758943}.
CC -!- FUNCTION: May act as a regulator of the RCS-phosphorelay signal
CC transduction pathway. {ECO:0000269|PubMed:11758943}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
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DR EMBL; U49400; AAC34720.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74401.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76401.1; -; Genomic_DNA.
DR PIR; B64881; B64881.
DR RefSeq; NP_415835.1; NC_000913.3.
DR RefSeq; WP_000735257.1; NZ_SSZK01000012.1.
DR PDB; 2F1C; X-ray; 2.30 A; X=22-301.
DR PDB; 2IWV; X-ray; 2.30 A; A/B/C/D=22-301.
DR PDB; 2IWW; X-ray; 2.70 A; A/B=22-301.
DR PDB; 2JQY; NMR; -; A=22-301.
DR PDB; 2WVP; X-ray; 2.40 A; A=22-301.
DR PDB; 2X9K; X-ray; 2.18 A; A=22-301.
DR PDB; 4CTD; X-ray; 3.20 A; A/B=22-301.
DR PDB; 5MWV; NMR; -; A=22-301.
DR PDB; 6OQH; NMR; -; A=22-301.
DR PDBsum; 2F1C; -.
DR PDBsum; 2IWV; -.
DR PDBsum; 2IWW; -.
DR PDBsum; 2JQY; -.
DR PDBsum; 2WVP; -.
DR PDBsum; 2X9K; -.
DR PDBsum; 4CTD; -.
DR PDBsum; 5MWV; -.
DR PDBsum; 6OQH; -.
DR AlphaFoldDB; P76045; -.
DR BMRB; P76045; -.
DR SMR; P76045; -.
DR BioGRID; 4260146; 153.
DR DIP; DIP-10399N; -.
DR IntAct; P76045; 1.
DR STRING; 511145.b1319; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 1.B.21.1.1; the ompg porin (ompg) family.
DR PaxDb; P76045; -.
DR PRIDE; P76045; -.
DR EnsemblBacteria; AAC74401; AAC74401; b1319.
DR EnsemblBacteria; BAE76401; BAE76401; BAE76401.
DR GeneID; 66674853; -.
DR GeneID; 945889; -.
DR KEGG; ecj:JW1312; -.
DR KEGG; eco:b1319; -.
DR PATRIC; fig|1411691.4.peg.959; -.
DR EchoBASE; EB3202; -.
DR eggNOG; ENOG502Z9QU; Bacteria.
DR HOGENOM; CLU_079589_0_0_6; -.
DR OMA; GYHYVNE; -.
DR BioCyc; EcoCyc:G6657-MON; -.
DR EvolutionaryTrace; P76045; -.
DR PRO; PR:P76045; -.
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:EcoCyc.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015481; F:maltose transporting porin activity; IDA:EcoCyc.
DR GO; GO:0015478; F:oligosaccharide transporting porin activity; IDA:EcoCyc.
DR GO; GO:0015288; F:porin activity; IMP:EcoliWiki.
DR GO; GO:0034219; P:carbohydrate transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR018981; Outer_membrane_porin_G.
DR Pfam; PF09381; Porin_OmpG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Ion transport; Membrane; Porin; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:9721282"
FT CHAIN 22..301
FT /note="Outer membrane porin G"
FT /id="PRO_0000025198"
FT TRANSMEM 27..35
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..57
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..72
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..98
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..112
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..136
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..158
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..182
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..195
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..209
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..222
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..238
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..248
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..265
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..279
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..300
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:2JQY"
FT STRAND 28..42
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 45..60
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 62..75
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:2X9K"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5MWV"
FT STRAND 86..118
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 127..160
FT /evidence="ECO:0007829|PDB:2X9K"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 169..181
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 183..198
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:2F1C"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 225..239
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:2X9K"
FT STRAND 266..280
FT /evidence="ECO:0007829|PDB:2X9K"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2WVP"
FT STRAND 289..300
FT /evidence="ECO:0007829|PDB:2X9K"
SQ SEQUENCE 301 AA; 34913 MW; 63D1234F3DCCFECF CRC64;
MKKLLPCTAL VMCAGMACAQ AEERNDWHFN IGAMYEIENV EGYGEDMDGL AEPSVYFNAA
NGPWRIALAY YQEGPVDYSA GKRGTWFDRP ELEVHYQFLE NDDFSFGLTG GFRNYGYHYV
DEPGKDTANM QRWKIAPDWD VKLTDDLRFN GWLSMYKFAN DLNTTGYADT RVETETGLQY
TFNETVALRV NYYLERGFNM DDSRNNGEFS TQEIRAYLPL TLGNHSVTPY TRIGLDRWSN
WDWQDDIERE GHDFNRVGLF YGYDFQNGLS VSLEYAFEWQ DHDEGDSDKF HYAGVGVNYS
F
