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Protein

Outer membrane protein C

Gene

ompC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Forms pores that allow passive diffusion of small molecules across the outer membrane.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi340 – 3401Magnesium; via carbonyl oxygen
Metal bindingi342 – 3421Magnesium; via carbonyl oxygen
Metal bindingi355 – 3551Magnesium; via carbonyl oxygen

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • ion transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Porin

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10670-MONOMER.
ECOL316407:JW2203-MONOMER.
MetaCyc:EG10670-MONOMER.

Protein family/group databases

TCDBi1.B.1.1.3. the general bacterial porin (gbp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Outer membrane protein C
Alternative name(s):
Outer membrane protein 1B
Porin OmpC
Gene namesi
Name:ompC
Synonyms:meoA, par
Ordered Locus Names:b2215, JW2203
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10670. ompC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 3312Periplasmic1 PublicationAdd
BLAST
Transmembranei34 – 429Beta stranded
Topological domaini43 – 5311Extracellular1 PublicationAdd
BLAST
Transmembranei54 – 6310Beta stranded
Topological domaini64 – 7310Periplasmic1 Publication
Transmembranei74 – 8411Beta strandedAdd
BLAST
Topological domaini85 – 917Extracellular1 Publication
Transmembranei92 – 10110Beta stranded
Topological domaini102 – 1065Periplasmic1 Publication
Transmembranei107 – 1159Beta stranded
Topological domaini116 – 14126Extracellular1 PublicationAdd
BLAST
Transmembranei142 – 15413Beta strandedAdd
BLAST
Topological domaini155 – 1639Periplasmic1 Publication
Transmembranei164 – 1718Beta stranded
Topological domaini172 – 20029Extracellular1 PublicationAdd
BLAST
Transmembranei201 – 2077Beta stranded
Topological domaini208 – 2114Periplasmic1 Publication
Transmembranei212 – 2198Beta stranded
Topological domaini220 – 24122Extracellular1 PublicationAdd
BLAST
Transmembranei242 – 2487Beta stranded
Topological domaini249 – 2524Periplasmic1 Publication
Transmembranei253 – 2608Beta stranded
Topological domaini261 – 2699Extracellular1 Publication
Transmembranei270 – 28617Beta strandedAdd
BLAST
Topological domaini287 – 2915Periplasmic1 Publication
Transmembranei292 – 2998Beta stranded
Topological domaini300 – 31819Extracellular1 PublicationAdd
BLAST
Transmembranei319 – 3268Beta stranded
Topological domaini327 – 3304Periplasmic1 Publication
Transmembranei331 – 3388Beta stranded
Topological domaini339 – 35820Extracellular1 PublicationAdd
BLAST
Transmembranei359 – 3668Beta stranded
Topological domaini367 – 3671Periplasmic1 Publication

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • integral component of cell outer membrane Source: EcoliWiki
  • pore complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21213 PublicationsAdd
BLAST
Chaini22 – 367346Outer membrane protein CPRO_0000025230Add
BLAST

Proteomic databases

PaxDbiP06996.
PRIDEiP06996.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi4261917. 276 interactions.
DIPiDIP-10397N.
IntActiP06996. 8 interactions.
MINTiMINT-1248362.
STRINGi511145.b2215.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 275Combined sources
Beta strandi30 – 4415Combined sources
Turni48 – 503Combined sources
Beta strandi56 – 8530Combined sources
Beta strandi92 – 10312Combined sources
Turni104 – 1063Combined sources
Beta strandi107 – 1159Combined sources
Helixi119 – 1224Combined sources
Helixi123 – 1253Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi143 – 15513Combined sources
Helixi156 – 1594Combined sources
Beta strandi164 – 1718Combined sources
Beta strandi176 – 1827Combined sources
Beta strandi184 – 1863Combined sources
Helixi193 – 1953Combined sources
Beta strandi200 – 20910Combined sources
Beta strandi212 – 22211Combined sources
Turni225 – 2273Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi237 – 25014Combined sources
Beta strandi253 – 26412Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi275 – 28612Combined sources
Beta strandi291 – 30515Combined sources
Turni308 – 3103Combined sources
Beta strandi312 – 34029Combined sources
Helixi346 – 3516Combined sources
Beta strandi358 – 36710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J1NX-ray2.00A/B/C22-367[»]
2J4UX-ray2.99P/Q/R/U/V/W22-367[»]
2ZLEelectron microscopy28.00D22-367[»]
3NB3electron microscopy-D22-367[»]
4A8Delectron microscopy28.00M22-366[»]
ProteinModelPortaliP06996.
SMRiP06996. Positions 22-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06996.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 13318Loop L3; may constrict the poreAdd
BLAST

Domaini

Loop L3 (residues 116-133) extends along the inner side of the beta barrel wall and may constrict the pore mid-length.1 Publication

Sequence similaritiesi

Belongs to the Gram-negative porin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105FCK. Bacteria.
COG3203. LUCA.
HOGENOMiHOG000272406.
InParanoidiP06996.
KOiK09475.
OMAiRTDEQNN.
OrthoDBiEOG65J4ZQ.
PhylomeDBiP06996.

Family and domain databases

Gene3Di2.40.160.10. 1 hit.
InterProiIPR023614. Porin_dom.
IPR001897. Porin_gammaproteobac.
IPR001702. Porin_Gram-ve.
IPR013793. Porin_Gram-ve_CS.
[Graphical view]
PfamiPF00267. Porin_1. 1 hit.
[Graphical view]
PRINTSiPR00183. ECOLIPORIN.
PR00182. ECOLNEIPORIN.
PROSITEiPS00576. GRAM_NEG_PORIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06996-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVKVLSLLV PALLVAGAAN AAEVYNKDGN KLDLYGKVDG LHYFSDNKDV
60 70 80 90 100
DGDQTYMRLG FKGETQVTDQ LTGYGQWEYQ IQGNSAENEN NSWTRVAFAG
110 120 130 140 150
LKFQDVGSFD YGRNYGVVYD VTSWTDVLPE FGGDTYGSDN FMQQRGNGFA
160 170 180 190 200
TYRNTDFFGL VDGLNFAVQY QGKNGNPSGE GFTSGVTNNG RDALRQNGDG
210 220 230 240 250
VGGSITYDYE GFGIGGAISS SKRTDAQNTA AYIGNGDRAE TYTGGLKYDA
260 270 280 290 300
NNIYLAAQYT QTYNATRVGS LGWANKAQNF EAVAQYQFDF GLRPSLAYLQ
310 320 330 340 350
SKGKNLGRGY DDEDILKYVD VGATYYFNKN MSTYVDYKIN LLDDNQFTRD
360
AGINTDNIVA LGLVYQF
Length:367
Mass (Da):40,368
Last modified:April 1, 1988 - v1
Checksum:i6A49370CC8A1A225
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00541 Genomic DNA. Translation: AAA24243.1.
U00096 Genomic DNA. Translation: AAC75275.1.
AP009048 Genomic DNA. Translation: BAA15998.1.
U00008 Genomic DNA. Translation: AAA16412.1.
PIRiA20867. MMECPC.
RefSeqiNP_416719.1. NC_000913.3.
WP_000865568.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75275; AAC75275; b2215.
BAA15998; BAA15998; BAA15998.
GeneIDi946716.
KEGGiecj:JW2203.
eco:b2215.
PATRICi32119789. VBIEscCol129921_2304.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00541 Genomic DNA. Translation: AAA24243.1.
U00096 Genomic DNA. Translation: AAC75275.1.
AP009048 Genomic DNA. Translation: BAA15998.1.
U00008 Genomic DNA. Translation: AAA16412.1.
PIRiA20867. MMECPC.
RefSeqiNP_416719.1. NC_000913.3.
WP_000865568.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J1NX-ray2.00A/B/C22-367[»]
2J4UX-ray2.99P/Q/R/U/V/W22-367[»]
2ZLEelectron microscopy28.00D22-367[»]
3NB3electron microscopy-D22-367[»]
4A8Delectron microscopy28.00M22-366[»]
ProteinModelPortaliP06996.
SMRiP06996. Positions 22-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261917. 276 interactions.
DIPiDIP-10397N.
IntActiP06996. 8 interactions.
MINTiMINT-1248362.
STRINGi511145.b2215.

Protein family/group databases

TCDBi1.B.1.1.3. the general bacterial porin (gbp) family.

Proteomic databases

PaxDbiP06996.
PRIDEiP06996.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75275; AAC75275; b2215.
BAA15998; BAA15998; BAA15998.
GeneIDi946716.
KEGGiecj:JW2203.
eco:b2215.
PATRICi32119789. VBIEscCol129921_2304.

Organism-specific databases

EchoBASEiEB0664.
EcoGeneiEG10670. ompC.

Phylogenomic databases

eggNOGiENOG4105FCK. Bacteria.
COG3203. LUCA.
HOGENOMiHOG000272406.
InParanoidiP06996.
KOiK09475.
OMAiRTDEQNN.
OrthoDBiEOG65J4ZQ.
PhylomeDBiP06996.

Enzyme and pathway databases

BioCyciEcoCyc:EG10670-MONOMER.
ECOL316407:JW2203-MONOMER.
MetaCyc:EG10670-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP06996.
PROiP06996.

Family and domain databases

Gene3Di2.40.160.10. 1 hit.
InterProiIPR023614. Porin_dom.
IPR001897. Porin_gammaproteobac.
IPR001702. Porin_Gram-ve.
IPR013793. Porin_Gram-ve_CS.
[Graphical view]
PfamiPF00267. Porin_1. 1 hit.
[Graphical view]
PRINTSiPR00183. ECOLIPORIN.
PR00182. ECOLNEIPORIN.
PROSITEiPS00576. GRAM_NEG_PORIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A comparative study on the genes for three porins of the Escherichia coli outer membrane. DNA sequence of the osmoregulated ompC gene."
    Mizuno T., Chou M.-Y., Inouye M.
    J. Biol. Chem. 258:6932-6940(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Automated multiplex sequencing of the E.coli genome."
    Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 218-367.
    Strain: K12 / BHB2600.
  6. "DNA sequence of the promoter region of the ompC gene and the amino acid sequence of the signal peptide of pro-OmpC protein of Escherichia coli."
    Mizuno T., Chou M.-Y., Inouye M.
    FEBS Lett. 151:159-164(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22, PROTEIN SEQUENCE OF 22-40.
  7. "Construction of a series of ompF-ompC chimeric genes by in vivo homologous recombination in Escherichia coli and characterization of the translational products."
    Nogami T., Mizuno T., Mizushima S.
    J. Bacteriol. 164:797-801(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-57.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-30.
    Strain: K12 / EMG2.
  9. "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis."
    Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.
    Electrophoresis 19:837-844(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-26.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  11. "Crystal structure of osmoporin OmpC from E. coli at 2.0 A."
    Basle A., Rummel G., Storici P., Rosenbusch J.P., Schirmer T.
    J. Mol. Biol. 362:933-942(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-367 IN COMPLEX WITH MG(2+), SUBUNIT, DOMAIN, TOPOLOGY.
  12. "Crystal structure of the membrane protein Ompc complex with antibacterial lactoferrin."
    Baalaji S., Acharya R.K., Singh T.P., Krishnaswamy S.
    Submitted (SEP-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 22-367.

Entry informationi

Entry nameiOMPC_ECOLI
AccessioniPrimary (citable) accession number: P06996
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: January 20, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds 1 Mg2+ per subunit; could be Ca2+ in vivo.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.