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Protein

Outer membrane protein OprM

Gene

oprM

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 18MKRSF…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 BLAST18
Mutagenesisi18C → G, F or W: No palmitoylation occurs. The protein functions normally in antibiotic efflux. 1 Publication1
Mutagenesisi142 – 147Missing : No protein produced. 1 Publication6
Mutagenesisi162 – 170Missing : No protein produced. 1 Publication9
Mutagenesisi216 – 226Missing : A non-functional protein is produced. 1 PublicationAdd BLAST11
Mutagenesisi295 – 303Missing : A non-functional protein is produced. 1 Publication9
Mutagenesisi334 – 343Missing : No protein produced. 1 Publication10
Mutagenesisi358 – 366Missing : No protein produced. 1 Publication9
Mutagenesisi462 – 467Missing : No protein produced. 1 Publication6

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17PROSITE-ProRule annotationAdd BLAST17
ChainiPRO_000003099918 – 485Outer membrane protein OprMAdd BLAST468

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi18N-palmitoyl cysteinePROSITE-ProRule annotation1 Publication1
Lipidationi18S-diacylglycerol cysteine1 Publication1

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

1485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni52 – 54Combined sources3
Helixi57 – 60Combined sources4
Helixi64 – 76Combined sources13
Helixi78 – 99Combined sources22
Beta strandi105 – 116Combined sources12
Turni118 – 120Combined sources3
Beta strandi121 – 125Combined sources5
Beta strandi127 – 143Combined sources17
Helixi148 – 213Combined sources66
Turni214 – 216Combined sources3
Helixi220 – 255Combined sources36
Helixi282 – 284Combined sources3
Helixi285 – 288Combined sources4
Helixi290 – 310Combined sources21
Beta strandi316 – 330Combined sources15
Beta strandi333 – 335Combined sources3
Beta strandi339 – 352Combined sources14
Helixi356 – 422Combined sources67
Helixi428 – 463Combined sources36

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
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 differs from that shown. Contaminating sequence. Vector contamination due to cloning in a phagemid vector.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti464 – 485GGGWN…EDPQA → WGGDCFDTCQKRAG in AAA74435 (PubMed:8226684).CuratedAdd BLAST22

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
PDB 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.
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.
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...

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: November 2, 2016
This is version 129 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.