UniProtKB - P0A910 (OMPA_ECOLI)
Outer membrane protein A
ompA
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 PublicationsRequired 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 PublicationsSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 73 | Part of salt bridge gating mechanism1 Publication | 1 | |
Sitei | 159 | Part of salt bridge gating mechanism1 Publication | 1 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- ion transmembrane transporter activity Source: EcoCyc
- porin activity Source: EcoliWiki
GO - Biological processi
- cellular response to DNA damage stimulus Source: EcoliWiki
- conjugation Source: EcoliWiki
- detection of virus Source: EcoliWiki
- ion transport Source: EcoliWiki
- viral entry into host cell Source: EcoliWiki
Keywordsi
Molecular function | Porin |
Biological process | Conjugation, Host-virus interaction, Ion transport, Transport |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10669-MONOMER |
Protein family/group databases
TCDBi | 1.B.6.1.1, the ompa-ompf porin (oop) family |
Names & Taxonomyi
Protein namesi | Recommended name: Outer membrane protein A1 PublicationUniRule annotationShort 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 |
Gene namesi | Name:ompA1 PublicationUniRule annotation Synonyms:con1 Publication, tolG1 Publication, tut1 Publication Ordered Locus Names:b0957, JW0940 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
- Cell outer membrane UniRule annotation1 Publication6 Publications; Multi-pass membrane protein UniRule annotation1 Publication7 Publications
Note: The 8 beta strands are tilted by about 45 degrees relative to the membrane normal (PubMed:9808047, PubMed:10764596, PubMed:11276254, PubMed:16719475). Evenly distributed on the outer membrane (PubMed:10947984).5 Publications
Other locations
- cell outer membrane Source: EcoliWiki
- integral component of cell outer membrane Source: EcoCyc
- integral component of membrane Source: EcoliWiki
- membrane Source: EcoliWiki
- outer membrane Source: EcoliWiki
- outer membrane-bounded periplasmic space Source: EcoCyc
- pore complex Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 22 – 26 | Periplasmic2 Publications | 5 | |
Transmembranei | 27 – 37 | Beta stranded2 PublicationsAdd BLAST | 11 | |
Topological domaini | 38 – 54 | Extracellular2 PublicationsAdd BLAST | 17 | |
Transmembranei | 55 – 66 | Beta stranded2 PublicationsAdd BLAST | 12 | |
Topological domaini | 67 – 69 | Periplasmic2 Publications | 3 | |
Transmembranei | 70 – 78 | Beta stranded2 Publications | 9 | |
Topological domaini | 79 – 95 | Extracellular2 PublicationsAdd BLAST | 17 | |
Transmembranei | 96 – 107 | Beta stranded2 PublicationsAdd BLAST | 12 | |
Topological domaini | 108 – 111 | Periplasmic2 Publications | 4 | |
Transmembranei | 112 – 120 | Beta stranded1 Publication1 Publication | 9 | |
Topological domaini | 121 – 141 | Extracellular1 Publication1 PublicationAdd BLAST | 21 | |
Transmembranei | 142 – 151 | Beta stranded1 Publication1 Publication | 10 | |
Topological domaini | 152 – 155 | Periplasmic2 Publications | 4 | |
Transmembranei | 156 – 164 | Beta stranded2 Publications | 9 | |
Topological domaini | 165 – 181 | Extracellular1 Publication1 PublicationAdd BLAST | 17 | |
Transmembranei | 182 – 191 | Beta stranded2 Publications | 10 | |
Topological domaini | 192 – 346 | Periplasmic2 PublicationsAdd BLAST | 155 |
Keywords - Cellular componenti
Cell outer membrane, MembranePathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 45 | I → 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 Publication | 1 | |
Mutagenesisi | 49 | G → 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 Publication | 1 | |
Mutagenesisi | 73 – 103 | EMGYD…QLTAK → CMGYDWLGRMPYKGSVENGA YKAQGVQLTAC: Nearly normal growth in absence of NaCl, reducing agent (0.05% beta-mercaptoethanol) has no effect. 1 PublicationAdd BLAST | 31 | |
Mutagenesisi | 73 | E → 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 Publication | 1 | |
Mutagenesisi | 73 | E → Q: Higher channel activity; channel is open longer and more often than wild-type, conductance does not change. 1 Publication | 1 | |
Mutagenesisi | 86 | G → D: Becomes sensitive to phages K3, K4, K3h1, M1, partially sensitive to phages TuII*-6, TuII*-24, K5 Ac3, Ox3, TuII-26, Ox4. 2 Publications | 1 | |
Mutagenesisi | 86 | G → R: Becomes sensitive to phages K3h1, partially sensitive to phages K4, K5, M1. Increased resistance to colicin K. 1 Publication | 1 | |
Mutagenesisi | 89 | E → G: Becomes partially sensitive to phages K3h1, M1. Increased resistance to colicin K. 1 Publication | 1 | |
Mutagenesisi | 89 | E → K: Becomes partially sensitive to phage M1. Increased resistance to colicin L. 2 Publications | 1 | |
Mutagenesisi | 89 | Missing : Becomes partially sensitive to phage M1. 1 Publication | 1 | |
Mutagenesisi | 91 | G → C: Becomes sensitive to phages K3, K4, K5, K3h1, TuII*-26, partially sensitive to phages TuII*-46, TuII*-24, TuII*-6, M1, Ox2h5. 1 Publication | 1 | |
Mutagenesisi | 91 | G → D: Becomes sensitive to phages K4, K5, K3h1, partially sensitive to phages TuII*-6, TuII*-24, K3, M1. 2 Publications | 1 | |
Mutagenesisi | 91 | G → R or V: Becomes partially sensitive to phages K3h1, M1. 2 Publications | 1 | |
Mutagenesisi | 103 | K → A: Decreased channel activity; channel opens less time and less often than wild-type. 1 Publication | 1 | |
Mutagenesisi | 126 – 127 | Missing : Becomes sensitive to phages Ox2, Ox4, Ox5. Increased resistance to colicin L. 1 Publication | 2 | |
Mutagenesisi | 128 | K → Y: Greatly improves X-ray-grade crystals. 1 Publication | 1 | |
Mutagenesisi | 128 | K → Y: Restores resistance to SDS, high salt, acid and cholate. 1 Publication | 1 | |
Mutagenesisi | 129 | S → F: Becomes sensitive to phages K3, K4, K5, K3h1, TuII*-26, Ox2, Ox4, Ox5, Ox2h5, Ox2h20, partially sensitive to phages TuII*-46, M1. 1 Publication | 1 | |
Mutagenesisi | 129 | S → P: Becomes sensitive to phages K3, K4, K5, K3h1, TuII*-26, Ox2h5, Ox2h20. 1 Publication | 1 | |
Mutagenesisi | 130 | N → I: Restores resistance to SDS, high salt, acid and cholate. 1 Publication | 1 | |
Mutagenesisi | 131 | V → D: Becomes sensitive to phage K3h1, Ox2h5, Ox2h20, partially sensitive to phages Ox2, Ox4, Ox5, M1. Increased resistance to colicin L. 2 Publications | 1 | |
Mutagenesisi | 149 | E → A or Q: Wild-type channel activity. 1 Publication | 1 | |
Mutagenesisi | 159 | R → A: Higher channel activity; channel is open longer and more often than wild-type, conductance does not change. 1 Publication | 1 | |
Mutagenesisi | 159 | R → 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 Publication | 1 | |
Mutagenesisi | 175 | G → 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 Publications | 1 | |
Mutagenesisi | 183 – 188 | LSLGVS → GSLGVG: No longer hydroxybutyrated. 1 Publication | 6 | |
Mutagenesisi | 184 – 187 | SLGV → GLGS: No longer hydroxybutyrated. 1 Publication | 4 | |
Mutagenesisi | 184 | S → 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 Publications | 1 | |
Mutagenesisi | 185 – 188 | LGVS → GGVG: No longer hydroxybutyrated. 1 Publication | 4 | |
Mutagenesisi | 188 | S → G: Protein is hydroxybutyrated. Reconstituted pores have lower conductance. No longer hydroxybutyrated, unable to form pores; when associated with G-184. 2 Publications | 1 | |
Mutagenesisi | 189 | Y → F: Protein is hydroxybutyrated. 1 Publication | 1 | |
Mutagenesisi | 190 | R → D or N: Protein is hydroxybutyrated. 1 Publication | 1 | |
Mutagenesisi | 213 | K → A: No longer dimerizes. 1 Publication | 1 | |
Mutagenesisi | 248 – 346 | Missing : No longer dimerizes. 1 PublicationAdd BLAST | 99 | |
Mutagenesisi | 294 – 346 | Missing : Still dimerizes. 1 PublicationAdd BLAST | 53 | |
Mutagenesisi | 311 | C → G: Protein insertion into vesicles is not blocked by ferricyanide. 1 Publication | 1 | |
Mutagenesisi | 338 | K → A: Still dimerizes. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04233, (Hydroxyethyloxy)Tri(Ethyloxy)Octane |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | 4 PublicationsAdd BLAST | 21 | |
ChainiPRO_0000020094 | 22 – 346 | Outer membrane protein AAdd BLAST | 325 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 184 | O3-poly(beta-hydroxybutyryl)serine1 Publication | 1 | |
Modified residuei | 188 | O3-poly(beta-hydroxybutyryl)serine1 Publication | 1 | |
Disulfide bondi | 311 ↔ 323 | 2 Publications1 Publication |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, HydroxylationProteomic databases
jPOSTi | P0A910 |
PaxDbi | P0A910 |
PRIDEi | P0A910 |
2D gel databases
SWISS-2DPAGEi | P0A910 |
PTM databases
CarbonylDBi | P0A910 |
Interactioni
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 PublicationsBinary interactionsi
P0A910
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4260032, 1011 interactors 849945, 1 interactor |
DIPi | DIP-31879N |
IntActi | P0A910, 18 interactors |
MINTi | P0A910 |
STRINGi | 511145.b0957 |
Structurei
Secondary structure
3D structure databases
BMRBi | P0A910 |
SMRi | P0A910 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A910 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 201 – 202 | 1 | 2 | |
Repeati | 203 – 204 | 2 | 2 | |
Repeati | 205 – 206 | 3 | 2 | |
Repeati | 207 – 208 | 4 | 2 | |
Domaini | 210 – 338 | OmpA-likeUniRule annotationAdd BLAST | 129 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 197 – 208 | Hinge-likeAdd BLAST | 12 | |
Regioni | 201 – 208 | 4 X 2 AA tandem repeats of A-P | 8 | |
Regioni | 209 – 297 | Required for dimerization1 PublicationAdd BLAST | 89 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Signal, Transmembrane, Transmembrane beta strandPhylogenomic databases
eggNOGi | COG2885, Bacteria COG3637, Bacteria |
HOGENOMi | CLU_031536_0_0_6 |
InParanoidi | P0A910 |
PhylomeDBi | P0A910 |
Family and domain databases
CDDi | cd07185, OmpA_C-like, 1 hit |
Gene3Di | 3.30.1330.60, 1 hit |
HAMAPi | MF_00842, OmpA, 1 hit |
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 |
Pfami | View protein in Pfam PF00691, OmpA, 1 hit PF01389, OmpA_membrane, 1 hit |
PRINTSi | PR01021, OMPADOMAIN PR01022, OUTRMMBRANEA |
SUPFAMi | SSF103088, SSF103088, 1 hit SSF56925, SSF56925, 1 hit |
PROSITEi | View protein in PROSITE PS01068, OMPA_1, 1 hit PS51123, OMPA_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Mass spectrometryi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 114 | I → V in strain: K1 / E44. 1 Publication | 1 |
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 |
PIRi | A93707, MMECA |
RefSeqi | NP_415477.1, NC_000913.3 WP_000750416.1, NZ_SSZK01000002.1 |
Genome annotation databases
EnsemblBacteriai | AAC74043; AAC74043; b0957 BAA35715; BAA35715; BAA35715 |
GeneIDi | 945571 |
KEGGi | ecj:JW0940 eco:b0957 |
PATRICi | fig|1411691.4.peg.1317 |
Similar proteinsi
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 |
PIRi | A93707, MMECA |
RefSeqi | NP_415477.1, NC_000913.3 WP_000750416.1, NZ_SSZK01000002.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BXW | X-ray | 2.50 | A | 21-192 | [»] | |
1G90 | NMR | - | A | 22-197 | [»] | |
1QJP | X-ray | 1.65 | A | 22-192 | [»] | |
2GE4 | NMR | - | A | 22-197 | [»] | |
2JMM | NMR | - | A | 23-197 | [»] | |
2MQE | NMR | - | A | 201-346 | [»] | |
3JBU | electron microscopy | 3.64 | z | 1-24 | [»] | |
5M2Q | X-ray | 1.70 | A/B | 1-22 | [»] | |
6ITC | electron microscopy | 3.45 | B | 2-26 | [»] | |
6LYR | X-ray | 3.28 | P | 180-188 | [»] | |
BMRBi | P0A910 | |||||
SMRi | P0A910 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260032, 1011 interactors 849945, 1 interactor |
DIPi | DIP-31879N |
IntActi | P0A910, 18 interactors |
MINTi | P0A910 |
STRINGi | 511145.b0957 |
Chemistry databases
DrugBanki | DB04233, (Hydroxyethyloxy)Tri(Ethyloxy)Octane |
Protein family/group databases
TCDBi | 1.B.6.1.1, the ompa-ompf porin (oop) family |
PTM databases
CarbonylDBi | P0A910 |
2D gel databases
SWISS-2DPAGEi | P0A910 |
Proteomic databases
jPOSTi | P0A910 |
PaxDbi | P0A910 |
PRIDEi | P0A910 |
Genome annotation databases
EnsemblBacteriai | AAC74043; AAC74043; b0957 BAA35715; BAA35715; BAA35715 |
GeneIDi | 945571 |
KEGGi | ecj:JW0940 eco:b0957 |
PATRICi | fig|1411691.4.peg.1317 |
Organism-specific databases
EchoBASEi | EB0663 |
Phylogenomic databases
eggNOGi | COG2885, Bacteria COG3637, Bacteria |
HOGENOMi | CLU_031536_0_0_6 |
InParanoidi | P0A910 |
PhylomeDBi | P0A910 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10669-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A910 |
PROi | PR:P0A910 |
Family and domain databases
CDDi | cd07185, OmpA_C-like, 1 hit |
Gene3Di | 3.30.1330.60, 1 hit |
HAMAPi | MF_00842, OmpA, 1 hit |
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 |
Pfami | View protein in Pfam PF00691, OmpA, 1 hit PF01389, OmpA_membrane, 1 hit |
PRINTSi | PR01021, OMPADOMAIN PR01022, OUTRMMBRANEA |
SUPFAMi | SSF103088, SSF103088, 1 hit SSF56925, SSF56925, 1 hit |
PROSITEi | View protein in PROSITE PS01068, OMPA_1, 1 hit PS51123, OMPA_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | OMPA_ECOLI | |
Accessioni | P0A910Primary (citable) accession number: P0A910 Secondary accession number(s): P02934 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 21, 1986 | |
Last modified: | February 23, 2022 | |
This is version 144 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families