OPRM_PSEAE
ID OPRM_PSEAE Reviewed; 485 AA.
AC Q51487; Q51444; Q9ZNM1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Outer membrane protein OprM;
DE Flags: Precursor;
GN Name=oprM; Synonyms=oprK; OrderedLocusNames=PA0427;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 73-80, AND FUNCTION
RP AS AN ANTIBIOTIC EFFLUX PUMP.
RC STRAIN=PAO6609;
RX PubMed=8226684; DOI=10.1128/jb.175.22.7363-7372.1993;
RA Poole K., Krebes K., McNally C., Neshat S.;
RT "Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for
RT involvement of an efflux operon.";
RL J. Bacteriol. 175:7363-7372(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, DIACYLGLYCEROL AT
RP CYS-18, PALMITOYLATION AT CYS-18, AND MUTAGENESIS OF CYS-18.
RC STRAIN=PAO4290;
RX PubMed=10889211; DOI=10.1074/jbc.m005742200;
RA Nakajima A., Sugimoto Y., Yoneyama H., Nakae T.;
RT "Localization of the outer membrane subunit OprM of resistance-nodulation-
RT cell division family multicomponent efflux pump in Pseudomonas
RT aeruginosa.";
RL J. Biol. Chem. 275:30064-30068(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296.
RC STRAIN=PAO6609;
RX PubMed=7968531; DOI=10.1111/j.1365-2958.1993.tb00925.x;
RA Poole K., Heinrichs D.E., Neshat S.;
RT "Cloning and sequence analysis of an EnvCD homologue in Pseudomonas
RT aeruginosa: regulation by iron and possible involvement in the secretion of
RT the siderophore pyoverdine.";
RL Mol. Microbiol. 10:529-544(1993).
RN [5]
RP PROTEIN SEQUENCE OF 151-168; 289-310; 329-358 AND 378-393, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15253424; DOI=10.1021/pr034074w;
RA Blonder J., Goshe M.B., Xiao W., Camp D.G. II, Wingerd M., Davis R.W.,
RA Smith R.D.;
RT "Global analysis of the membrane subproteome of Pseudomonas aeruginosa
RT using liquid chromatography-tandem mass spectrometry.";
RL J. Proteome Res. 3:434-444(2004).
RN [6]
RP FUNCTION IN ANTIBIOTIC EFFLUX AND ENERGETIC REQUIREMENTS.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8540696; DOI=10.1128/aac.39.9.1948;
RA Li X.-Z., Nikaido H., Poole K.;
RT "Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa.";
RL Antimicrob. Agents Chemother. 39:1948-1953(1995).
RN [7]
RP FUNCTION IN MEXCD PUMP.
RC STRAIN=ML5087;
RX PubMed=9401051; DOI=10.1128/jb.179.24.7875-7881.1997;
RA Srikumar R., Li X.-Z., Poole K.;
RT "Inner membrane efflux components are responsible for beta-lactam
RT specificity of multidrug efflux pumps in Pseudomonas aeruginosa.";
RL J. Bacteriol. 179:7875-7881(1997).
RN [8]
RP FUNCTION IN SOLVENT EFFLUX.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9603892; DOI=10.1128/jb.180.11.2987-2991.1998;
RA Li X.-Z., Zhang L., Poole K.;
RT "Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic
RT solvent tolerance.";
RL J. Bacteriol. 180:2987-2991(1998).
RN [9]
RP FUNCTION IN MEXXY EFFLUX SYSTEM.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10952562; DOI=10.1128/aac.44.9.2242-2246.2000;
RA Masuda N., Sakagawa E., Ohya S., Gotoh N., Tsujimoto H., Nishino T.;
RT "Contribution of the MexX-MexY-oprM efflux system to intrinsic resistance
RT in Pseudomonas aeruginosa.";
RL Antimicrob. Agents Chemother. 44:2242-2246(2000).
RN [10]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF THE SIGNAL SEQUENCE, AND MUTAGENESIS
RP OF CONSERVED AMINO ACIDS AND REGIONS.
RC STRAIN=ML5087;
RX PubMed=11114896; DOI=10.1128/jb.183.1.12-27.2001;
RA Li X.-Z., Poole K.;
RT "Mutational analysis of the OprM outer membrane component of the MexA-MexB-
RT OprM multidrug efflux system of Pseudomonas aeruginosa.";
RL J. Bacteriol. 183:12-27(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 18-485.
RC STRAIN=PAO4290;
RX PubMed=15507433; DOI=10.1074/jbc.c400445200;
RA Akama H., Kanemaki M., Yoshimura M., Tsukihara T., Kashiwagi T.,
RA Yoneyama H., Narita S., Nakagawa A., Nakae T.;
RT "Crystal structure of the drug discharge outer membrane protein, OprM, of
RT Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded
RT cavity end.";
RL J. Biol. Chem. 279:52816-52819(2004).
RN [12]
RP TWO-DIMENSIONAL ELECTRON CRYSTALLOGRAPHY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15797729; DOI=10.1016/j.jsb.2005.01.001;
RA Lambert O., Benabdelhak H., Chami M., Jouan L., Nouaille E., Ducruix A.,
RA Brisson A.;
RT "Trimeric structure of OprN and OprM efflux proteins from Pseudomonas
RT aeruginosa, by 2D electron crystallography.";
RL J. Struct. Biol. 150:50-57(2005).
CC -!- FUNCTION: The outer membrane component of the MexAB-OprM efflux system
CC that confers multidrug resistance. Also functions as the major efflux
CC pump for n-hexane and p-xylene efflux. Over-expression of the pump
CC increases antibiotic and solvent efflux capacities. Can replace the
CC OprJ outer membrane component of the MexCD-OprJ pump; the antibiotics
CC exported are those exported by the intact MexCD pump, showing that
CC efflux substrate specificity is not conferred by this component. Serves
CC as the outer membrane component for the MexXY efflux system. Implicated
CC in the secretion of the siderophore pyoverdine. OprM is probably
CC involved in the efflux of the siderophore across the outer membrane.
CC -!- FUNCTION: The ability to export antibiotics and solvents is
CC dramatically decreased in the presence of the proton conductor carbonyl
CC cyanide m-chlorophenylhydrazone (CCCP), showing that an energized inner
CC membrane is required for efflux. It is thought that the MexB subunit is
CC a proton antiporter.
CC -!- SUBUNIT: Component of the MexAB-OprM multidrug efflux complex composed
CC of an unknown number of MexA subunits, MexB and an OprM homotrimer. The
CC OprM homotrimer assembles to form a 135 Angstroms-long pore. It
CC consists of a beta-barrel, which is probably inserted in the outer
CC membrane, and an alpha-barrel formed by alpha-helices which probably
CC spans the periplasm. In the ground state the periplasmic end is closed,
CC while the outer membrane end opening is 6-8 Angstroms in diameter. The
CC OprM trimer is thought to contact the inner membrane MexB transporter.
CC The MexA subunits are thought to form a barrel which allows substrates
CC to pass directly from the cytoplasm to the external mileu. How the MexA
CC subunits interact with OprM and MexB, and how the OprM channel is
CC opened is unknown.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:10889211,
CC ECO:0000269|PubMed:11114896}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:10889211,
CC ECO:0000269|PubMed:11114896}. Note=Attached to the outer membrane by a
CC lipid anchor and via the transmembrane beta-barrel. The membrane anchor
CC is not necessary for antibiotic efflux. In one report (PubMed:10889211)
CC the Cys-18-Gly mutant is reported to be periplasmically located, in
CC another (PubMed:11114896) the same protein is reported to be located in
CC the outer membrane. {ECO:0000269|PubMed:10889211,
CC ECO:0000269|PubMed:11114896}.
CC -!- INDUCTION: By growth under severe iron limitation.
CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74435.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination due to cloning in a phagemid vector.; Evidence={ECO:0000305};
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DR EMBL; L23839; AAA74435.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB011381; BAA28694.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03816.1; -; Genomic_DNA.
DR EMBL; L11616; AAA74438.1; -; Genomic_DNA.
DR PIR; A49937; A49937.
DR PIR; F83593; F83593.
DR RefSeq; NP_249118.1; NC_002516.2.
DR RefSeq; WP_003084633.1; NZ_QZGE01000016.1.
DR PDB; 1WP1; X-ray; 2.56 A; A/B=18-485.
DR PDB; 3D5K; X-ray; 2.40 A; A/B/C=18-485.
DR PDB; 4Y1K; X-ray; 3.80 A; A/B/C/D/E/F=18-485.
DR PDB; 6IOK; EM; 3.64 A; A/B/C=18-485.
DR PDB; 6IOL; EM; 3.76 A; A/B/C=18-485.
DR PDB; 6TA5; EM; 3.20 A; A/B/C=18-485.
DR PDB; 6TA6; EM; 3.20 A; A/B/C=18-485.
DR PDB; 6ZRE; X-ray; 2.80 A; A/B=18-485.
DR PDB; 7AKZ; X-ray; 3.20 A; A/B=18-485.
DR PDBsum; 1WP1; -.
DR PDBsum; 3D5K; -.
DR PDBsum; 4Y1K; -.
DR PDBsum; 6IOK; -.
DR PDBsum; 6IOL; -.
DR PDBsum; 6TA5; -.
DR PDBsum; 6TA6; -.
DR PDBsum; 6ZRE; -.
DR PDBsum; 7AKZ; -.
DR AlphaFoldDB; Q51487; -.
DR SMR; Q51487; -.
DR STRING; 287.DR97_3395; -.
DR ChEMBL; CHEMBL4523990; -.
DR ChEMBL; CHEMBL4523991; -.
DR DrugBank; DB14879; Cefiderocol.
DR TCDB; 2.A.6.2.21; the resistance-nodulation-cell division (rnd) superfamily.
DR PaxDb; Q51487; -.
DR PRIDE; Q51487; -.
DR EnsemblBacteria; AAG03816; AAG03816; PA0427.
DR GeneID; 877851; -.
DR KEGG; pae:PA0427; -.
DR PATRIC; fig|208964.12.peg.449; -.
DR PseudoCAP; PA0427; -.
DR HOGENOM; CLU_012817_13_3_6; -.
DR InParanoid; Q51487; -.
DR OMA; AANQDYY; -.
DR PhylomeDB; Q51487; -.
DR BioCyc; PAER208964:G1FZ6-431-MON; -.
DR EvolutionaryTrace; Q51487; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR003423; OMP_efflux.
DR InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT.
DR Pfam; PF02321; OEP; 2.
DR TIGRFAMs; TIGR01845; outer_NodT; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell outer membrane;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..485
FT /note="Outer membrane protein OprM"
FT /id="PRO_0000030999"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:10889211"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:10889211"
FT MUTAGEN 1..18
FT /note="MKRSFLSLAVAAVVLSGC->MKLKNTLGVVIGSLVAASAMNAFAQG:
FT Replaces the endogenous lipoprotein signal by the signal
FT for the outer membrane protein OprF. A functional outer
FT membrane targeted protein is made."
FT /evidence="ECO:0000269|PubMed:11114896"
FT MUTAGEN 18
FT /note="C->G,F,W: No palmitoylation occurs. The protein
FT functions normally in antibiotic efflux."
FT /evidence="ECO:0000269|PubMed:10889211"
FT MUTAGEN 142..147
FT /note="Missing: No protein produced."
FT /evidence="ECO:0000269|PubMed:11114896"
FT MUTAGEN 162..170
FT /note="Missing: No protein produced."
FT /evidence="ECO:0000269|PubMed:11114896"
FT MUTAGEN 216..226
FT /note="Missing: A non-functional protein is produced."
FT /evidence="ECO:0000269|PubMed:11114896"
FT MUTAGEN 295..303
FT /note="Missing: A non-functional protein is produced."
FT /evidence="ECO:0000269|PubMed:11114896"
FT MUTAGEN 334..343
FT /note="Missing: No protein produced."
FT /evidence="ECO:0000269|PubMed:11114896"
FT MUTAGEN 358..366
FT /note="Missing: No protein produced."
FT /evidence="ECO:0000269|PubMed:11114896"
FT MUTAGEN 462..467
FT /note="Missing: No protein produced."
FT /evidence="ECO:0000269|PubMed:11114896"
FT CONFLICT 464..485
FT /note="GGGWNQQTVTQQQTAKKEDPQA -> WGGDCFDTCQKRAG (in Ref. 1;
FT AAA74435)"
FT /evidence="ECO:0000305"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6TA5"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3D5K"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3D5K"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:3D5K"
FT HELIX 78..99
FT /evidence="ECO:0007829|PDB:3D5K"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:3D5K"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3D5K"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3D5K"
FT STRAND 127..143
FT /evidence="ECO:0007829|PDB:3D5K"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6TA6"
FT HELIX 148..213
FT /evidence="ECO:0007829|PDB:3D5K"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3D5K"
FT HELIX 220..255
FT /evidence="ECO:0007829|PDB:3D5K"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6TA6"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3D5K"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:3D5K"
FT HELIX 290..310
FT /evidence="ECO:0007829|PDB:3D5K"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:6TA5"
FT STRAND 316..330
FT /evidence="ECO:0007829|PDB:3D5K"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3D5K"
FT STRAND 339..352
FT /evidence="ECO:0007829|PDB:3D5K"
FT HELIX 356..422
FT /evidence="ECO:0007829|PDB:3D5K"
FT HELIX 428..463
FT /evidence="ECO:0007829|PDB:3D5K"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:6ZRE"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6TA5"
SQ SEQUENCE 485 AA; 52598 MW; 7B0918E4FE7843EF CRC64;
MKRSFLSLAV AAVVLSGCSL IPDYQRPEAP VAAAYPQGQA YGQNTGAAAV PAADIGWREF
FRDPQLQQLI GVALENNRDL RVAALNVEAF RAQYRIQRAD LFPRIGVDGS GTRQRLPGDL
STTGSPAISS QYGVTLGTTA WELDLFGRLR SLRDQALEQY LATEQAQRSA QTTLVASVAT
AYLTLKADQA QLQLTKDTLG TYQKSFDLTQ RSYDVGVASA LDLRQAQTAV EGARATLAQY
TRLVAQDQNA LVLLLGSGIP ANLPQGLGLD QTLLTEVPAG LPSDLLQRRP DILEAEHQLM
AANASIGAAR AAFFPSISLT ANAGTMSRQL SGLFDAGSGS WLFQPSINLP IFTAGSLRAS
LDYAKIQKDI NVAQYEKAIQ TAFQEVADGL AARGTFTEQL QAQRDLVKAS DEYYQLADKR
YRTGVDNYLT LLDAQRSLFT AQQQLITDRL NQLTSEVNLY KALGGGWNQQ TVTQQQTAKK
EDPQA
