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ECOLI:OMPC
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | ompC (synonyms: meoA, par) | |
| Protein Name(s) | Outer membrane protein C
Outer membrane protein 1B Porin OmpC | |
| External Links | ||
| UniProt | P06996 | |
| EMBL | K00541 U00096 AP009048 U00008 | |
| PIR | A20867 | |
| RefSeq | NP_416719.1 YP_490453.1 | |
| PDB | 2J1N 2J4U 2ZLE 3NB3 4A8D | |
| PDBsum | 2J1N 2J4U 2ZLE 3NB3 4A8D | |
| ProteinModelPortal | P06996 | |
| SMR | P06996 | |
| DIP | DIP-10397N | |
| IntAct | P06996 | |
| MINT | MINT-1248362 | |
| STRING | 511145.b2215 | |
| TCDB | 1.B.1.1.3 | |
| PaxDb | P06996 | |
| PRIDE | P06996 | |
| EnsemblBacteria | AAC75275 BAA15998 | |
| GeneID | 12932923 946716 | |
| KEGG | ecj:Y75_p2176 eco:b2215 | |
| PATRIC | 32119789 | |
| EchoBASE | EB0664 | |
| EcoGene | EG10670 | |
| eggNOG | COG3203 | |
| HOGENOM | HOG000272406 | |
| InParanoid | P06996 | |
| KO | K09475 | |
| OMA | RTDEQNN | |
| OrthoDB | EOG65J4ZQ | |
| PhylomeDB | P06996 | |
| BioCyc | EcoCyc:EG10670-MONOMER ECOL316407:JW2203-MONOMER MetaCyc:EG10670-MONOMER | |
| EvolutionaryTrace | P06996 | |
| PRO | PR:P06996 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P06996 | |
| GO | GO:0045203 GO:0046930 GO:0046872 GO:0015288 GO:0006974 GO:0006811 | |
| Gene3D | 2.40.160.10 | |
| InterPro | IPR023614 IPR001897 IPR001702 IPR013793 | |
| Pfam | PF00267 | |
| PRINTS | PR00183 PR00182 | |
| PROSITE | PS00576 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0009279 |
cell outer membrane |
ECO:0000314 |
C |
Table 1 |
complete | |||||
| GO:0001618 |
virus receptor activity |
ECO:0007042 |
F |
Fig. 3B shows that ompC in E.coli is involved in the adsorption of the side tail fiber (stf) of bacteriophage lambda. |
complete | |||||
| GO:0046813 |
receptor-mediated virion attachment to host cell |
ECO:0007042 |
epifluorescence microscopy evidence used in manual assertion |
P |
Figure 3B shows that the presence of the ompC receptor in E. Coli causes the side tail fibers to strongly adsorb, which leads to less dark infection. |
complete | ||||
|
part_of |
GO:0045203 |
integral component of cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006974 |
cellular response to DNA damage stimulus |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0015914 |
phospholipid transport |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0015288 |
porin activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055085 |
transmembrane transport |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0015288 |
porin activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006811 |
ion transport |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0046930 |
pore complex |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Molloy, MP et al. (2000) Proteomic analysis of the Escherichia coli outer membrane. Eur. J. Biochem. 267 2871-81 PubMed GONUTS page
- ↑ 2.0 2.1 Guan, J et al. (2019) The role of side tail fibers during the infection cycle of phage lambda. Virology 527 57-63 PubMed GONUTS page
- ↑ Baslé, A et al. (2006) Crystal structure of osmoporin OmpC from E. coli at 2.0 A. J. Mol. Biol. 362 933-42 PubMed GONUTS page
- ↑ Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
- ↑ Chong, ZS et al. (2015) Osmoporin OmpC forms a complex with MlaA to maintain outer membrane lipid asymmetry in Escherichia coli. Mol. Microbiol. 98 1133-46 PubMed GONUTS page
- ↑ Han, MJ et al. (2012) Comparative analysis of envelope proteomes in Escherichia coli B and K-12 strains. J. Microbiol. Biotechnol. 22 470-8 PubMed GONUTS page
- ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
