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Protein

Outer membrane protein OprM

Gene

oprM

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The outer membrane component of the MexAB-OprM efflux system that confers multidrug resistance. Also functions as the major efflux pump for n-hexane and p-xylene efflux. Over-expression of the pump increases antibiotic and solvent efflux capacities. Can replace the OprJ outer membrane component of the MexCD-OprJ pump; the antibiotics exported are those exported by the intact MexCD pump, showing that efflux substrate specificity is not conferred by this component. Serves as the outer membrane component for the MexXY efflux system. Implicated in the secretion of the siderophore pyoverdine. OprM is probably involved in the efflux of the siderophore across the outer membrane.
The ability to export antibiotics and solvents is dramatically decreased in the presence of the proton conductor carbonyl cyanide m-chlorophenylhydrazone (CCCP), showing that an energized inner membrane is required for efflux. It is thought that the MexB subunit is a proton antiporter.

GO - Molecular functioni

  • drug transmembrane transporter activity Source: PseudoCAP
  • lipid binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Transport

Protein family/group databases

TCDBi2.A.6.2.21. the resistance-nodulation-cell division (rnd) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Outer membrane protein OprM
Gene namesi
Name:oprM
Synonyms:oprK
Ordered Locus Names:PA0427
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0427.

Subcellular locationi

  • Cell outer membrane 2 Publications; Lipid-anchor PROSITE-ProRule annotation2 Publications

  • Note: Attached to the outer membrane by a lipid anchor and via the transmembrane beta-barrel. The membrane anchor is not necessary for antibiotic efflux. In one report (PubMed:10889211) the Cys-18-Gly mutant is reported to be periplasmically located, in another (PubMed:11114896) the same protein is reported to be located in the outer membrane.2 Publications

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 1818MKRSF…VLSGC → MKLKNTLGVVIGSLVAASAM NAFAQG: Replaces the endogenous lipoprotein signal by the signal for the outer membrane protein OprF. A functional outer membrane targeted protein is made. 1 PublicationAdd
BLAST
Mutagenesisi18 – 181C → G, F or W: No palmitoylation occurs. The protein functions normally in antibiotic efflux. 1 Publication
Mutagenesisi142 – 1476Missing : No protein produced. 1 Publication
Mutagenesisi162 – 1709Missing : No protein produced. 1 Publication
Mutagenesisi216 – 22611Missing : A non-functional protein is produced. 1 PublicationAdd
BLAST
Mutagenesisi295 – 3039Missing : A non-functional protein is produced. 1 Publication
Mutagenesisi334 – 34310Missing : No protein produced. 1 Publication
Mutagenesisi358 – 3669Missing : No protein produced. 1 Publication
Mutagenesisi462 – 4676Missing : No protein produced. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717PROSITE-ProRule annotationAdd
BLAST
Chaini18 – 485468Outer membrane protein OprMPRO_0000030999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi18 – 181N-palmitoyl cysteinePROSITE-ProRule annotation1 Publication
Lipidationi18 – 181S-diacylglycerol cysteine1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ51487.
PRIDEiQ51487.

Expressioni

Inductioni

By growth under severe iron limitation.

Interactioni

Subunit structurei

Component of the MexAB-OprM multidrug efflux complex composed of an unknown number of MexA subunits, MexB and an OprM homotrimer. The OprM homotrimer assembles to form a 135 Angstroms-long pore. It consists of a beta-barrel, which is probably inserted in the outer membrane, and an alpha-barrel formed by alpha-helices which probably spans the periplasm. In the ground state the periplasmic end is closed, while the outer membrane end opening is 6-8 Angstroms in diameter. The OprM trimer is thought to contact the inner membrane MexB transporter. The MexA subunits are thought to form a barrel which allows substrates to pass directly from the cytoplasm to the external mileu. How the MexA subunits interact with OprM and MexB, and how the OprM channel is opened is unknown.

Protein-protein interaction databases

STRINGi208964.PA0427.

Structurei

Secondary structure

1
485
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni52 – 543Combined sources
Helixi57 – 604Combined sources
Helixi64 – 7613Combined sources
Helixi78 – 9922Combined sources
Beta strandi105 – 11612Combined sources
Turni118 – 1203Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi127 – 14317Combined sources
Helixi148 – 21366Combined sources
Turni214 – 2163Combined sources
Helixi220 – 25536Combined sources
Helixi282 – 2843Combined sources
Helixi285 – 2884Combined sources
Helixi290 – 31021Combined sources
Beta strandi316 – 33015Combined sources
Beta strandi333 – 3353Combined sources
Beta strandi339 – 35214Combined sources
Helixi356 – 42267Combined sources
Helixi428 – 46336Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WP1X-ray2.56A/B18-485[»]
3D5KX-ray2.40A/B/C18-485[»]
4Y1KX-ray3.80A/B/C/D/E/F18-485[»]
ProteinModelPortaliQ51487.
SMRiQ51487. Positions 19-472.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51487.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105ENJ. Bacteria.
COG1538. LUCA.
HOGENOMiHOG000111955.
InParanoidiQ51487.
KOiK18139.
OMAiMIESTRA.
OrthoDBiEOG6MWN87.
PhylomeDBiQ51487.

Family and domain databases

InterProiIPR003423. OMP_efflux.
IPR010131. RND_efflux_OM_lipoprot_NodT.
[Graphical view]
PfamiPF02321. OEP. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01845. outer_NodT. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q51487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSFLSLAV AAVVLSGCSL IPDYQRPEAP VAAAYPQGQA YGQNTGAAAV
60 70 80 90 100
PAADIGWREF FRDPQLQQLI GVALENNRDL RVAALNVEAF RAQYRIQRAD
110 120 130 140 150
LFPRIGVDGS GTRQRLPGDL STTGSPAISS QYGVTLGTTA WELDLFGRLR
160 170 180 190 200
SLRDQALEQY LATEQAQRSA QTTLVASVAT AYLTLKADQA QLQLTKDTLG
210 220 230 240 250
TYQKSFDLTQ RSYDVGVASA LDLRQAQTAV EGARATLAQY TRLVAQDQNA
260 270 280 290 300
LVLLLGSGIP ANLPQGLGLD QTLLTEVPAG LPSDLLQRRP DILEAEHQLM
310 320 330 340 350
AANASIGAAR AAFFPSISLT ANAGTMSRQL SGLFDAGSGS WLFQPSINLP
360 370 380 390 400
IFTAGSLRAS LDYAKIQKDI NVAQYEKAIQ TAFQEVADGL AARGTFTEQL
410 420 430 440 450
QAQRDLVKAS DEYYQLADKR YRTGVDNYLT LLDAQRSLFT AQQQLITDRL
460 470 480
NQLTSEVNLY KALGGGWNQQ TVTQQQTAKK EDPQA
Length:485
Mass (Da):52,598
Last modified:December 8, 2000 - v2
Checksum:i7B0918E4FE7843EF
GO

Sequence cautioni

The sequence AAA74435.1 differs from that shown.Contaminating sequence. Vector contamination due to cloning in a phagemid vector.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 48522GGGWN…EDPQA → WGGDCFDTCQKRAG in AAA74435 (PubMed:8226684).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23839 Genomic DNA. Translation: AAA74435.1. Sequence problems.
AB011381 Genomic DNA. Translation: BAA28694.1.
AE004091 Genomic DNA. Translation: AAG03816.1.
L11616 Genomic DNA. Translation: AAA74438.1.
PIRiA49937.
F83593.
RefSeqiNP_249118.1. NC_002516.2.
WP_003084633.1. NZ_ASJY01000084.1.

Genome annotation databases

EnsemblBacteriaiAAG03816; AAG03816; PA0427.
GeneIDi877851.
KEGGipae:PA0427.
PATRICi19835096. VBIPseAer58763_0449.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23839 Genomic DNA. Translation: AAA74435.1. Sequence problems.
AB011381 Genomic DNA. Translation: BAA28694.1.
AE004091 Genomic DNA. Translation: AAG03816.1.
L11616 Genomic DNA. Translation: AAA74438.1.
PIRiA49937.
F83593.
RefSeqiNP_249118.1. NC_002516.2.
WP_003084633.1. NZ_ASJY01000084.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WP1X-ray2.56A/B18-485[»]
3D5KX-ray2.40A/B/C18-485[»]
4Y1KX-ray3.80A/B/C/D/E/F18-485[»]
ProteinModelPortaliQ51487.
SMRiQ51487. Positions 19-472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA0427.

Protein family/group databases

TCDBi2.A.6.2.21. the resistance-nodulation-cell division (rnd) superfamily.

Proteomic databases

PaxDbiQ51487.
PRIDEiQ51487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG03816; AAG03816; PA0427.
GeneIDi877851.
KEGGipae:PA0427.
PATRICi19835096. VBIPseAer58763_0449.

Organism-specific databases

PseudoCAPiPA0427.

Phylogenomic databases

eggNOGiENOG4105ENJ. Bacteria.
COG1538. LUCA.
HOGENOMiHOG000111955.
InParanoidiQ51487.
KOiK18139.
OMAiMIESTRA.
OrthoDBiEOG6MWN87.
PhylomeDBiQ51487.

Miscellaneous databases

EvolutionaryTraceiQ51487.

Family and domain databases

InterProiIPR003423. OMP_efflux.
IPR010131. RND_efflux_OM_lipoprot_NodT.
[Graphical view]
PfamiPF02321. OEP. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01845. outer_NodT. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon."
    Poole K., Krebes K., McNally C., Neshat S.
    J. Bacteriol. 175:7363-7372(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 73-80, FUNCTION AS AN ANTIBIOTIC EFFLUX PUMP.
    Strain: PAO6609.
  2. "Localization of the outer membrane subunit OprM of resistance-nodulation-cell division family multicomponent efflux pump in Pseudomonas aeruginosa."
    Nakajima A., Sugimoto Y., Yoneyama H., Nakae T.
    J. Biol. Chem. 275:30064-30068(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, DIACYLGLYCEROL AT CYS-18, PALMITOYLATION AT CYS-18, MUTAGENESIS OF CYS-18.
    Strain: PAO4290.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  4. "Cloning and sequence analysis of an EnvCD homologue in Pseudomonas aeruginosa: regulation by iron and possible involvement in the secretion of the siderophore pyoverdine."
    Poole K., Heinrichs D.E., Neshat S.
    Mol. Microbiol. 10:529-544(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296.
    Strain: PAO6609.
  5. "Global analysis of the membrane subproteome of Pseudomonas aeruginosa using liquid chromatography-tandem mass spectrometry."
    Blonder J., Goshe M.B., Xiao W., Camp D.G. II, Wingerd M., Davis R.W., Smith R.D.
    J. Proteome Res. 3:434-444(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 151-168; 289-310; 329-358 AND 378-393, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  6. "Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa."
    Li X.-Z., Nikaido H., Poole K.
    Antimicrob. Agents Chemother. 39:1948-1953(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANTIBIOTIC EFFLUX AND ENERGETIC REQUIREMENTS.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  7. "Inner membrane efflux components are responsible for beta-lactam specificity of multidrug efflux pumps in Pseudomonas aeruginosa."
    Srikumar R., Li X.-Z., Poole K.
    J. Bacteriol. 179:7875-7881(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEXCD PUMP.
    Strain: ML5087.
  8. "Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic solvent tolerance."
    Li X.-Z., Zhang L., Poole K.
    J. Bacteriol. 180:2987-2991(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SOLVENT EFFLUX.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  9. "Contribution of the MexX-MexY-oprM efflux system to intrinsic resistance in Pseudomonas aeruginosa."
    Masuda N., Sakagawa E., Ohya S., Gotoh N., Tsujimoto H., Nishino T.
    Antimicrob. Agents Chemother. 44:2242-2246(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEXXY EFFLUX SYSTEM.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  10. "Mutational analysis of the OprM outer membrane component of the MexA-MexB-OprM multidrug efflux system of Pseudomonas aeruginosa."
    Li X.-Z., Poole K.
    J. Bacteriol. 183:12-27(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF THE SIGNAL SEQUENCE, MUTAGENESIS OF CONSERVED AMINO ACIDS AND REGIONS.
    Strain: ML5087.
  11. "Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end."
    Akama H., Kanemaki M., Yoshimura M., Tsukihara T., Kashiwagi T., Yoneyama H., Narita S., Nakagawa A., Nakae T.
    J. Biol. Chem. 279:52816-52819(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 18-485.
    Strain: PAO4290.
  12. "Trimeric structure of OprN and OprM efflux proteins from Pseudomonas aeruginosa, by 2D electron crystallography."
    Lambert O., Benabdelhak H., Chami M., Jouan L., Nouaille E., Ducruix A., Brisson A.
    J. Struct. Biol. 150:50-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TWO-DIMENSIONAL ELECTRON CRYSTALLOGRAPHY.
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiOPRM_PSEAE
AccessioniPrimary (citable) accession number: Q51487
Secondary accession number(s): Q51444, Q9ZNM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 8, 2000
Last modified: July 6, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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.