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ECOLI:OMPA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ompA (synonyms: con, tolG, tut)
Protein Name(s) Outer membrane protein A

Outer membrane protein II*

External Links
UniProt P0A910
EMBL V00307
U00096
AP009048
PIR A93707
RefSeq NP_415477.1
YP_489229.1
PDB 1BXW
1G90
1QJP
2GE4
2JMM
3NB3
PDBsum 1BXW
1G90
1QJP
2GE4
2JMM
3NB3
ProteinModelPortal P0A910
SMR P0A910
DIP DIP-31879N
IntAct P0A910
MINT MINT-1308131
STRING 511145.b0957
TCDB 1.B.6.1.1
SWISS-2DPAGE P0A910
PaxDb P0A910
PRIDE P0A910
EnsemblBacteria AAC74043
BAA35715
GeneID 12931038
945571
KEGG ecj:Y75_p0929
eco:b0957
PATRIC 32117133
EchoBASE EB0663
EcoGene EG10669
eggNOG COG2885
HOGENOM HOG000274199
InParanoid P0A910
KO K03286
OMA EYALTKN
OrthoDB EOG6PP9QB
BioCyc EcoCyc:EG10669-MONOMER
ECOL316407:JW0940-MONOMER
EvolutionaryTrace P0A910
PRO PR:P0A910
Proteomes UP000000318
UP000000625
Genevestigator P0A910
GO GO:0009279
GO:0016021
GO:0016020
GO:0019867
GO:0046930
GO:0015288
GO:0005198
GO:0006974
GO:0000746
GO:0009597
GO:0034220
GO:0006811
GO:0006810
GO:0046718
Gene3D 2.40.160.20
3.30.1330.60
InterPro IPR011250
IPR006664
IPR002368
IPR006690
IPR000498
IPR006665
Pfam PF00691
PF01389
PRINTS PR01021
PR01022
SUPFAM SSF103088
SSF56925
PROSITE PS01068
PS51123

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009279

cell outer membrane

PMID:10806384[1]

ECO:0000314

C

Table 1

complete

part_of

GO:0009279

cell outer membrane

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10669
EcoGene:EG10684
PANTHER:PTN002013697
UniProtKB:P02936

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24746938[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A910

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16079137[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A910

F

Seeded From UniProt

complete

involved_in

GO:0046718

viral entry into host cell

PMID:367782[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0019867

outer membrane

PMID:3047120[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0019867

outer membrane

PMID:12509434[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

PMID:3047121[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

PMID:12509434[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:12509434[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0015288

porin activity

PMID:10636850[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009597

detection of virus

PMID:367782[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:3047120[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:20081027[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:12509434[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:11967071[11]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006811

ion transport

PMID:10636850[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000746

conjugation

PMID:3311813[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0046930

pore complex

PMID:1370823[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0046930

pore complex

PMID:10764596[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0034220

ion transmembrane transport

PMID:10636850[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0015288

porin activity

PMID:1370823[13]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0015288

porin activity

PMID:10636850[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005198

structural molecule activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002368

F

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000498
InterPro:IPR002368
InterPro:IPR006664
InterPro:IPR006690

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000498
InterPro:IPR002368
InterPro:IPR006664
InterPro:IPR006690

C

Seeded From UniProt

complete

involved_in

GO:0006811

ion transport

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0406

P

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0998
UniProtKB-SubCell:SL-0040

C

Seeded From UniProt

complete

enables

GO:0015288

porin activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0626

F

Seeded From UniProt

complete

involved_in

GO:0000746

conjugation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0184

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0046930

pore complex

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0626

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Molloy, MP et al. (2000) Proteomic analysis of the Escherichia coli outer membrane. Eur. J. Biochem. 267 2871-81 PubMed GONUTS page
  2. ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ Marcoux, J et al. (2014) Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA. Structure 22 781-90 PubMed GONUTS page
  4. ↑ Stenberg, F et al. (2005) Protein complexes of the Escherichia coli cell envelope. J. Biol. Chem. 280 34409-19 PubMed GONUTS page
  5. ↑ 5.0 5.1 Henning, U et al. (1978) Mutants (ompA) affecting a major outer membrane protein of Escherichia coli K12. Eur. J. Biochem. 92 491-8 PubMed GONUTS page
  6. ↑ 6.0 6.1 Klose, M et al. (1988) Internal deletions in the gene for an Escherichia coli outer membrane protein define an area possibly important for recognition of the outer membrane by this polypeptide. J. Biol. Chem. 263 13291-6 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 7.3 Bulieris, PV et al. (2003) Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 278 9092-9 PubMed GONUTS page
  8. ↑ Klose, M et al. (1988) The influence of amino substitutions within the mature part of an Escherichia coli outer membrane protein (OmpA) on assembly of the polypeptide into its membrane. J. Biol. Chem. 263 13297-302 PubMed GONUTS page
  9. ↑ 9.0 9.1 9.2 9.3 Arora, A et al. (2000) Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers. J. Biol. Chem. 275 1594-600 PubMed GONUTS page
  10. ↑ Arutyunov, D et al. (2010) F plasmid TraF and TraH are components of an outer membrane complex involved in conjugation. J. Bacteriol. 192 1730-4 PubMed GONUTS page
  11. ↑ 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
  12. ↑ Ried, G & Henning, U (1987) A unique amino acid substitution in the outer membrane protein OmpA causes conjugation deficiency in Escherichia coli K-12. FEBS Lett. 223 387-90 PubMed GONUTS page
  13. ↑ 13.0 13.1 Sugawara, E & Nikaido, H (1992) Pore-forming activity of OmpA protein of Escherichia coli. J. Biol. Chem. 267 2507-11 PubMed GONUTS page
  14. ↑ Pautsch, A & Schulz, GE (2000) High-resolution structure of the OmpA membrane domain. J. Mol. Biol. 298 273-82 PubMed GONUTS page
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