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Entry version 130 (31 Jul 2019)
Sequence version 1 (21 Jul 1986)
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Protein

Outer membrane protein A

Gene

ompA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape (PubMed:11906175, PubMed:361695). Non-covalently binds peptidoglycan (PubMed:25135663) (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes (PubMed:1370823, PubMed:20004640, PubMed:21069910). A very abundant protein, there can be up to 210,000 OmpA molecules per cell (PubMed:24766808). Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, which allows diffusion of L-arabinose at a rate comparable to that of OmpF porin; the pores interconvert very rarely (PubMed:7517935). Native and reconstituted protein forms ion channels with 2 conductance states of (50-80 pS) and (260-320 pS); the states are interconvertible in this study. Interconversion requires refolding of the periplasmic domain (PubMed:10636850). Small pores are converted into large pores by increasing temperature; in this model the C-terminal periplasmic domain forms 8 more beta sheets to form a larger pore (PubMed:15850404). The center of the isolated beta-barrel is polar and has a central gate (involving Glu-73, Lys-103, Glu-149 and Arg-159, sandwiched between Tyr-29, Phe-40 and Tyr-94), with no obvious passage for water or ions (PubMed:9808047) (Probable). Gating involves the Glu-73-Arg-159 salt bridge; gate opening probably involves formation of alternate salt bridges Glu-149-Arg-159 and Glu-73-Lys-103 (PubMed:17041590). Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan maintains the position of the cell wall in the periplasm, holding it approximately equidistant from both the inner and outer membranes. Trimeric Lpp controls the width of the periplasm, adjusts its tilt angle to accommodate to the available space, and can compensate in part for an absence of OmpA (Probable).4 Publications12 Publications
Required for F plasmid cell conjugation; purified protein plus lipopolysaccharide (LPS) inhibits conjugation in a concentration-dependent manner. OmpA probably acts as the receptor on recipient cells (PubMed:321438) (Probable). Required for the stabilization of mating aggregates during F plasmid conjugative transfer, may interact with F plasmid-encoded TraN, but not with TraN from plasmid R100-1 (PubMed:9696748, PubMed:16272376). All 4 external, surface-exposed loops are required for F plasmid conjugation (PubMed:10368142).1 Publication4 Publications
(Microbial infection) Mutants with decreased or altered protein are resistant to bacteriophage TuII* (PubMed:1107069, PubMed:791936). Mutants which have no or greatly reduced protein levels are resistant to a number of bacteriophages, including K3, K4, K5, Ox2, Ox3, Ox4, Ox5, Ml, and Ac3 (Probable) (PubMed:783129, PubMed:3902787). Mutations in this protein render the bacteria partially or completely susceptible to a number of bacteriophages for which is it probably the receptor (PubMed:6086577, PubMed:3902787). All but the last external, surface-exposed loops are required for phage K3 infection (PubMed:10368142).1 Publication6 Publications
(Microbial infection) A mutation in this locus (called tolG) renders the cell tolerant to bacteriocin JF246 but does not affect its sensitivity to colicins A, C, El, E2, E3, K, Ia, or Ib (PubMed:4591955). Mutations in this protein render the bacteria partially or completely susceptible to colicin K or colicin L, for which is it probably the receptor (PubMed:6086577).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei73Part of salt bridge gating mechanism1 Publication1
Sitei159Part of salt bridge gating mechanism1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionPorin
Biological processConjugation, Host-virus interaction, Ion transport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
EcoCyc:EG10669-MONOMER
ECOL316407:JW0940-MONOMER

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.B.6.1.1 the ompa-ompf porin (oop) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Outer membrane protein A1 PublicationUniRule annotation
Short name:
OmpA
Alternative name(s):
Outer membrane porin AUniRule annotation
Outer membrane protein 3A1 Publication
Outer membrane protein B
Outer membrane protein II*
Outer membrane protein d
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ompA1 PublicationUniRule annotation
Synonyms:con1 Publication, tolG1 Publication, tut1 Publication
Ordered Locus Names:b0957, JW0940
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10669 ompA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini22 – 26Periplasmic2 Publications5
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei27 – 37Beta stranded2 PublicationsAdd BLAST11
Topological domaini38 – 54Extracellular2 PublicationsAdd BLAST17
Transmembranei55 – 66Beta stranded2 PublicationsAdd BLAST12
Topological domaini67 – 69Periplasmic2 Publications3
Transmembranei70 – 78Beta stranded2 Publications9
Topological domaini79 – 95Extracellular2 PublicationsAdd BLAST17
Transmembranei96 – 107Beta stranded2 PublicationsAdd BLAST12
Topological domaini108 – 111Periplasmic2 Publications4
Transmembranei112 – 120Beta stranded1 Publication1 Publication9
Topological domaini121 – 141Extracellular1 Publication1 PublicationAdd BLAST21
Transmembranei142 – 151Beta stranded1 Publication1 Publication10
Topological domaini152 – 155Periplasmic2 Publications4
Transmembranei156 – 164Beta stranded2 Publications9
Topological domaini165 – 181Extracellular1 Publication1 PublicationAdd BLAST17
Transmembranei182 – 191Beta stranded2 Publications10
Topological domaini192 – 346Periplasmic2 PublicationsAdd BLAST155

GO - Cellular componenti

Keywords - Cellular componenti

Cell outer membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Double lpp-ompA mutants are spherical and only grow in the presence of electrolytes such as 30 mM Mg2+, and are sensitive to hydrophobic antibiotics and detergents. The peptidoglycan layer is no longer attached to the cell outer membrane which undergoes abundant blebbing (PubMed:361695). Decreased efficiency of bacterial conjugation of the F plasmid (PubMed:9696748). Deletions grow poorly on SDS, cholate, at pH 3.8 or at 5 M NaCl (PubMed:11906175). Grows very slowly in the absence of NaCl, wild-type growth in 1% NaCl (PubMed:17041590). E.coli is no longer killed by human neutrophil elastase (ELANE) in vitro (PubMed:10947984).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi45I → N: Becomes sensitive to phages K3, K4, K5, K3h1, AC3, Ox3, TuII*-24, TuII*-26, partially sensitive to phages TuII*-6, TuII*-60, M1. 1 Publication1
Mutagenesisi49G → V: Becomes sensitive to phages K3, K4, K5, K3h1, TuII*-24, TuII*-26, M1, Ox2h5, Ox2h20, partially sensitive to phages TuII*-46, TuII*-24, TuII*-6, AC3, Ox3. 1 Publication1
Mutagenesisi73 – 103EMGYD…QLTAK → CMGYDWLGRMPYKGSVENGA YKAQGVQLTAC: Nearly normal growth in absence of NaCl, reducing agent (0.05% beta-mercaptoethanol) has no effect. 1 PublicationAdd BLAST31
Mutagenesisi73E → C: Modifies gate residues, no activity in oxidizing conditions, in reducing conditions activity channel opens frequently, probably forms a disulfide cross-link in channel, grows very poorly in the absence of NaCl, reducing agent (0.05% beta-mercaptoethanol) improves growth; when associated with C-159. 1 Publication1
Mutagenesisi73E → Q: Higher channel activity; channel is open longer and more often than wild-type, conductance does not change. 1 Publication1
Mutagenesisi86G → D: Becomes sensitive to phages K3, K4, K3h1, M1, partially sensitive to phages TuII*-6, TuII*-24, K5 Ac3, Ox3, TuII-26, Ox4. 2 Publications1
Mutagenesisi86G → R: Becomes sensitive to phages K3h1, partially sensitive to phages K4, K5, M1. Increased resistance to colicin K. 1 Publication1
Mutagenesisi89E → G: Becomes partially sensitive to phages K3h1, M1. Increased resistance to colicin K. 1 Publication1
Mutagenesisi89E → K: Becomes partially sensitive to phage M1. Increased resistance to colicin L. 2 Publications1
Mutagenesisi89Missing : Becomes partially sensitive to phage M1. 1 Publication1
Mutagenesisi91G → C: Becomes sensitive to phages K3, K4, K5, K3h1, TuII*-26, partially sensitive to phages TuII*-46, TuII*-24, TuII*-6, M1, Ox2h5. 1 Publication1
Mutagenesisi91G → D: Becomes sensitive to phages K4, K5, K3h1, partially sensitive to phages TuII*-6, TuII*-24, K3, M1. 2 Publications1
Mutagenesisi91G → R or V: Becomes partially sensitive to phages K3h1, M1. 2 Publications1
Mutagenesisi103K → A: Decreased channel activity; channel opens less time and less often than wild-type. 1 Publication1
Mutagenesisi126 – 127Missing : Becomes sensitive to phages Ox2, Ox4, Ox5. Increased resistance to colicin L. 1 Publication2
Mutagenesisi128K → Y: Greatly improves X-ray-grade crystals. 1 Publication1
Mutagenesisi128K → Y: Restores resistance to SDS, high salt, acid and cholate. 1 Publication1
Mutagenesisi129S → F: Becomes sensitive to phages K3, K4, K5, K3h1, TuII*-26, Ox2, Ox4, Ox5, Ox2h5, Ox2h20, partially sensitive to phages TuII*-46, M1. 1 Publication1
Mutagenesisi129S → P: Becomes sensitive to phages K3, K4, K5, K3h1, TuII*-26, Ox2h5, Ox2h20. 1 Publication1
Mutagenesisi130N → I: Restores resistance to SDS, high salt, acid and cholate. 1 Publication1
Mutagenesisi131V → D: Becomes sensitive to phage K3h1, Ox2h5, Ox2h20, partially sensitive to phages Ox2, Ox4, Ox5, M1. Increased resistance to colicin L. 2 Publications1
Mutagenesisi149E → A or Q: Wild-type channel activity. 1 Publication1
Mutagenesisi159R → A: Higher channel activity; channel is open longer and more often than wild-type, conductance does not change. 1 Publication1
Mutagenesisi159R → C: Modifies gate residues, no activity in oxidizing conditions, in reducing conditions activity channel opens frequently, probably forms a disulfide cross-link in channel, grows very poorly in the absence of NaCl, addition of reducing agent (0.05% beta-mercaptoethanol) improves growth; when associated with C-173. 1 Publication1
Mutagenesisi175G → D or S: Becomes sensitive to phages TuII*-6, TuII*-24, TuII*-46, TuII-26, TuII*-60, K3, K4, K5, K3h1, Ac3, Ox3, M1. Increased resistance to colicins K and L. 2 Publications1
Mutagenesisi183 – 188LSLGVS → GSLGVG: No longer hydroxybutyrated. 1 Publication6
Mutagenesisi184 – 187SLGV → GLGS: No longer hydroxybutyrated. 1 Publication4
Mutagenesisi184S → G: Protein is hydroxybutyrated. Reconstituted pores have lower conductance and are open for less time. No longer hydroxybutyrated, unable to form pores; when associated with G-188. 2 Publications1
Mutagenesisi185 – 188LGVS → GGVG: No longer hydroxybutyrated. 1 Publication4
Mutagenesisi188S → G: Protein is hydroxybutyrated. Reconstituted pores have lower conductance. No longer hydroxybutyrated, unable to form pores; when associated with G-184. 2 Publications1
Mutagenesisi189Y → F: Protein is hydroxybutyrated. 1 Publication1
Mutagenesisi190R → D or N: Protein is hydroxybutyrated. 1 Publication1
Mutagenesisi213K → A: No longer dimerizes. 1 Publication1
Mutagenesisi248 – 346Missing : No longer dimerizes. 1 PublicationAdd BLAST99
Mutagenesisi294 – 346Missing : Still dimerizes. 1 PublicationAdd BLAST53
Mutagenesisi311C → G: Protein insertion into vesicles is not blocked by ferricyanide. 1 Publication1
Mutagenesisi338K → A: Still dimerizes. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 214 PublicationsAdd BLAST21
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002009422 – 346Outer membrane protein AAdd BLAST325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei184O3-poly(beta-hydroxybutyryl)serine1 Publication1
Modified residuei188O3-poly(beta-hydroxybutyryl)serine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi311 ↔ 3232 Publications1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Hydroxybutyrylation on Ser-184 and/or Ser-188 can add up to 10 R-3-hydroxybutyrate residues; it is not clear if one or both residues are modified in vivo. Hydrophobic residues adjacent to the modified Ser residues (i.e. Leu-183, Leu-185 and Val-187) are important for hydroxylation. Hydroxybutyrylation occurs in the cytoplasm (PubMed:17659252). Hydroxybutyrylation is required for stable pore formation, unmodified protein may not be able to insert into the outer membrane (PubMed:20004640). Further hydroxybutyrylation occurs in the C-terminal fragment (residues 285-346); this modification probably occurs in the periplasm (PubMed:21069910).3 Publications
OmpA is degraded by human neutrophil elastase (ELANE) in vitro; this coincides with bacterial death. Mice with a homozygous knockout of ELANE are more easily killed by wild-type E.coli but not by E.coli with an ompA deletion; this experiment was certainly not performed with E.coli strain K12 which is no longer virulent.Curated1 Publication

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P0A910

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0A910

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P0A910

PRoteomics IDEntifications database

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PRIDEi
P0A910

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P0A910

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P0A910

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:1370823, PubMed:10764596, PubMed:9808047). Homodimer (PubMed:16079137, PubMed:21697552, PubMed:24746938).

Interacts with Lpp (PubMed:3013869). About 10% of the C-terminal periplasmic domain dimerizes when expressed without the N-terminal domain (PubMed:25135663, PubMed:24746938).

Interacts with F plasmid-encoded TraN during conjugation (Probable) (PubMed:16272376).

1 Publication9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
4260032, 1011 interactors
849945, 1 interactor

Database of interacting proteins

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DIPi
DIP-31879N

Protein interaction database and analysis system

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IntActi
P0A910, 18 interactors

Molecular INTeraction database

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MINTi
P0A910

STRING: functional protein association networks

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STRINGi
511145.b0957

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P0A910

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P0A910

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati201 – 20212
Repeati203 – 20422
Repeati205 – 20632
Repeati207 – 20842
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini210 – 338OmpA-likeUniRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni197 – 208Hinge-likeAdd BLAST12
Regioni201 – 2084 X 2 AA tandem repeats of A-P8
Regioni209 – 297Required for dimerization1 PublicationAdd BLAST89

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminus transmembrane region forms low conductance pores (50-80 pS); larger conductance pores (260-320 pS) are formed by the whole protein. Refolding of the periplasmic domain may be required to make the large conductance pores (PubMed:10636850). The structure of the whole protein is controversial; the periplasmic domain may or may not be inserted into the cell outer membrane to form a larger pore. The protein with a narrow 8 sheet beta-barrel and a periplasmic domain may be an intermediate in formation of the larger pore (Probable). The disulfide bond is necessary for formation of the larger pore; disulfide-bonded protein inserts into the membrane without reduction (PubMed:2211627, PubMed:21069910). The isolated C-terminal periplasmic domain binds peptidoglycan (PubMed:25135663, PubMed:27866852). A region in the isolated periplasmic domain bulges from the rest of the protein (resides 302-328) and is stabilized by the disulfide bond (PubMed:25135663).3 Publications5 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpA family. [View classification]UniRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG4105UYK Bacteria
COG2885 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000274199

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0A910

KEGG Orthology (KO)

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KOi
K03286

Family and domain databases

Conserved Domains Database

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CDDi
cd07185 OmpA_C-like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.1330.60, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00842 OmpA, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011250 OMP/PagP_b-brl
IPR006664 OMP_bac
IPR002368 OmpA
IPR006665 OmpA-like
IPR006690 OMPA-like_CS
IPR036737 OmpA-like_sf
IPR000498 OmpA-like_TM_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00691 OmpA, 1 hit
PF01389 OmpA_membrane, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01021 OMPADOMAIN
PR01022 OUTRMMBRANEA

Superfamily database of structural and functional annotation

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SUPFAMi
SSF103088 SSF103088, 1 hit
SSF56925 SSF56925, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01068 OMPA_1, 1 hit
PS51123 OMPA_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A910-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKTAIAIAV ALAGFATVAQ AAPKDNTWYT GAKLGWSQYH DTGFINNNGP
60 70 80 90 100
THENQLGAGA FGGYQVNPYV GFEMGYDWLG RMPYKGSVEN GAYKAQGVQL
110 120 130 140 150
TAKLGYPITD DLDIYTRLGG MVWRADTKSN VYGKNHDTGV SPVFAGGVEY
160 170 180 190 200
AITPEIATRL EYQWTNNIGD AHTIGTRPDN GMLSLGVSYR FGQGEAAPVV
210 220 230 240 250
APAPAPAPEV QTKHFTLKSD VLFNFNKATL KPEGQAALDQ LYSQLSNLDP
260 270 280 290 300
KDGSVVVLGY TDRIGSDAYN QGLSERRAQS VVDYLISKGI PADKISARGM
310 320 330 340
GESNPVTGNT CDNVKQRAAL IDCLAPDRRV EIEVKGIKDV VTQPQA
Length:346
Mass (Da):37,201
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i195147734CDF8B04
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 35177 Da from positions 22 - 346. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti114I → V in strain K1 / E44. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
V00307 Genomic DNA Translation: CAA23588.1
U00096 Genomic DNA Translation: AAC74043.1
AP009048 Genomic DNA Translation: BAA35715.1

Protein sequence database of the Protein Information Resource

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PIRi
A93707 MMECA

NCBI Reference Sequences

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RefSeqi
NP_415477.1, NC_000913.3
WP_000750416.1, NZ_SSZK01000002.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAC74043; AAC74043; b0957
BAA35715; BAA35715; BAA35715

Database of genes from NCBI RefSeq genomes

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GeneIDi
945571

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ecj:JW0940
eco:b0957

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1317

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00307 Genomic DNA Translation: CAA23588.1
U00096 Genomic DNA Translation: AAC74043.1
AP009048 Genomic DNA Translation: BAA35715.1
PIRiA93707 MMECA
RefSeqiNP_415477.1, NC_000913.3
WP_000750416.1, NZ_SSZK01000002.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXWX-ray2.50A21-192[»]
1G90NMR-A22-197[»]
1QJPX-ray1.65A22-192[»]
2GE4NMR-A22-197[»]
2JMMNMR-A23-197[»]
2MQENMR-A201-346[»]
3JBUelectron microscopy3.64z1-24[»]
5M2QX-ray1.70A/B1-22[»]
SMRiP0A910
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4260032, 1011 interactors
849945, 1 interactor
DIPiDIP-31879N
IntActiP0A910, 18 interactors
MINTiP0A910
STRINGi511145.b0957

Chemistry databases

DrugBankiDB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane

Protein family/group databases

TCDBi1.B.6.1.1 the ompa-ompf porin (oop) family

PTM databases

CarbonylDBiP0A910

2D gel databases

SWISS-2DPAGEiP0A910

Proteomic databases

EPDiP0A910
jPOSTiP0A910
PaxDbiP0A910
PRIDEiP0A910

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74043; AAC74043; b0957
BAA35715; BAA35715; BAA35715
GeneIDi945571
KEGGiecj:JW0940
eco:b0957
PATRICifig|1411691.4.peg.1317

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0663
EcoGeneiEG10669 ompA

Phylogenomic databases

eggNOGiENOG4105UYK Bacteria
COG2885 LUCA
HOGENOMiHOG000274199
InParanoidiP0A910
KOiK03286

Enzyme and pathway databases

BioCyciEcoCyc:EG10669-MONOMER
ECOL316407:JW0940-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A910

Protein Ontology

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PROi
PR:P0A910

Family and domain databases

CDDicd07185 OmpA_C-like, 1 hit
Gene3Di3.30.1330.60, 1 hit
HAMAPiMF_00842 OmpA, 1 hit
InterProiView protein in InterPro
IPR011250 OMP/PagP_b-brl
IPR006664 OMP_bac
IPR002368 OmpA
IPR006665 OmpA-like
IPR006690 OMPA-like_CS
IPR036737 OmpA-like_sf
IPR000498 OmpA-like_TM_dom
PfamiView protein in Pfam
PF00691 OmpA, 1 hit
PF01389 OmpA_membrane, 1 hit
PRINTSiPR01021 OMPADOMAIN
PR01022 OUTRMMBRANEA
SUPFAMiSSF103088 SSF103088, 1 hit
SSF56925 SSF56925, 1 hit
PROSITEiView protein in PROSITE
PS01068 OMPA_1, 1 hit
PS51123 OMPA_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOMPA_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A910
Secondary accession number(s): P02934
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 31, 2019
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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