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| Accession Number: | Q51487 |
| Protein Name: | Outer membrane protein oprM [Precursor] |
| Length: | 485 |
| Molecular Weight: | 52598.00 |
| Species: | Pseudomonas aeruginosa [287] |
| Location1 / Topology2 / Orientation3: | Cell outer membrane1 / Lipid-anchor2 |
| Substrate | macrolide, fluoroquinolone antibiotic, ofloxacin, ciprofloxacin, chloramphenicol, beta-lactam, imipenem, tetracycline, amino cyclitol glycoside, erythromycin A, carbapenemcarboxylic acid |
Cross database links:
| RefSeq: | NP_249118.1 |
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| Entrez Gene ID: | 877851 |
| Pfam: | PF02321 |
| BioCyc: | PAER208964:PA0427-MONOMER |
| KEGG: | pae:PA0427 |
Gene Ontology
GO:0009279
C:cell outer membrane
GO:0016021
C:integral to membrane
GO:0005886
C:plasma membrane
GO:0008289
F:lipid binding
GO:0005215
F:transporter activity
GO:0046677
P:response to antibiotic
GO:0006810
P:transport
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References (12)[1] “Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon.” Poole K.et.al. 8226684 [2] “Localization of the outer membrane subunit OprM of resistance-nodulation-cell division family multicomponent efflux pump in Pseudomonas aeruginosa.” Nakajima A.et.al. 10889211 [3] “Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.” Stover C.K.et.al. 10984043 [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.et.al. 7968531 [5] “Global analysis of the membrane subproteome of Pseudomonas aeruginosa using liquid chromatography-tandem mass spectrometry.” Blonder J.et.al. 15253424 [6] “Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa.” Li X.-Z.et.al. 8540696 [7] “Inner membrane efflux components are responsible for beta-lactam specificity of multidrug efflux pumps in Pseudomonas aeruginosa.” Srikumar R.et.al. 9401051 [8] “Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic solvent tolerance.” Li X.-Z.et.al. 9603892 [9] “Contribution of the MexX-MexY-oprM efflux system to intrinsic resistance in Pseudomonas aeruginosa.” Masuda N.et.al. 10952562 [10] “Mutational analysis of the OprM outer membrane component of the MexA-MexB-OprM multidrug efflux system of Pseudomonas aeruginosa.” Li X.-Z.et.al. 11114896 [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.et.al. 15507433 [12] “Trimeric structure of OprN and OprM efflux proteins from Pseudomonas aeruginosa, by 2D electron crystallography.” Lambert O.et.al. 15797729
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| Structure: | |
External Searches:
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Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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1: MKRSFLSLAV AAVVLSGCSL IPDYQRPEAP VAAAYPQGQA YGQNTGAAAV PAADIGWREF 61: FRDPQLQQLI GVALENNRDL RVAALNVEAF RAQYRIQRAD LFPRIGVDGS GTRQRLPGDL 121: STTGSPAISS QYGVTLGTTA WELDLFGRLR SLRDQALEQY LATEQAQRSA QTTLVASVAT 181: AYLTLKADQA QLQLTKDTLG TYQKSFDLTQ RSYDVGVASA LDLRQAQTAV EGARATLAQY 241: TRLVAQDQNA LVLLLGSGIP ANLPQGLGLD QTLLTEVPAG LPSDLLQRRP DILEAEHQLM 301: AANASIGAAR AAFFPSISLT ANAGTMSRQL SGLFDAGSGS WLFQPSINLP IFTAGSLRAS 361: LDYAKIQKDI NVAQYEKAIQ TAFQEVADGL AARGTFTEQL QAQRDLVKAS DEYYQLADKR 421: YRTGVDNYLT LLDAQRSLFT AQQQLITDRL NQLTSEVNLY KALGGGWNQQ TVTQQQTAKK 481: EDPQA