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Multidrug resistance protein MexA

 MEXA_PSEAE              Reviewed;         383 AA.
P52477; Q9S506;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 121.
RecName: Full=Multidrug resistance protein MexA;
Flags: Precursor;
Name=mexA; OrderedLocusNames=PA0425;
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=208964;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=PAO6609;
PubMed=7968531; DOI=10.1111/j.1365-2958.1993.tb00925.x;
Poole K., Heinrichs D.E., Neshat S.;
"Cloning and sequence analysis of an EnvCD homologue in Pseudomonas
aeruginosa: regulation by iron and possible involvement in the
secretion of the siderophore pyoverdine.";
Mol. Microbiol. 10:529-544(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=10984043; DOI=10.1038/35023079;
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an
opportunistic pathogen.";
Nature 406:959-964(2000).
[3]
PROTEIN SEQUENCE OF 63-76; 87-119; 263-287 AND 327-359, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=15253424; DOI=10.1021/pr034074w;
Blonder J., Goshe M.B., Xiao W., Camp D.G. II, Wingerd M., Davis R.W.,
Smith R.D.;
"Global analysis of the membrane subproteome of Pseudomonas aeruginosa
using liquid chromatography-tandem mass spectrometry.";
J. Proteome Res. 3:434-444(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-383.
STRAIN=PA14;
PubMed=9989496; DOI=10.1016/S0092-8674(00)80958-7;
Mahajan-Miklos S., Tan M.-W., Rahme L.G., Ausubel F.M.;
"Molecular mechanisms of bacterial virulence elucidated using a
Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model.";
Cell 96:47-56(1999).
[5]
FUNCTION AS AN ANTIBIOTIC EFFLUX PUMP.
STRAIN=PAO6609;
PubMed=8226684; DOI=10.1128/jb.175.22.7363-7372.1993;
Poole K., Krebes K., McNally C., Neshat S.;
"Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence
for involvement of an efflux operon.";
J. Bacteriol. 175:7363-7372(1993).
[6]
FUNCTION IN ANTIBIOTIC EFFLUX, AND ENERGETIC REQUIREMENTS.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=8540696; DOI=10.1128/AAC.39.9.1948;
Li X.-Z., Nikaido H., Poole K.;
"Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas
aeruginosa.";
Antimicrob. Agents Chemother. 39:1948-1953(1995).
[7]
FUNCTION IN SOLVENT EFFLUX.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=9603892;
Li X.-Z., Zhang L., Poole K.;
"Role of the multidrug efflux systems of Pseudomonas aeruginosa in
organic solvent tolerance.";
J. Bacteriol. 180:2987-2991(1998).
[8]
SUBCELLULAR LOCATION, DIACYLGLYCEROL AT CYS-24, PALMITOYLATION AT
CYS-24, AND MUTAGENESIS OF CYS-24.
STRAIN=PAO4290;
PubMed=10671490; DOI=10.1074/jbc.275.7.4628;
Yoneyama H., Maseda H., Kamiguchi H., Nakae T.;
"Function of the membrane fusion protein, MexA, of the MexA, B-OprM
efflux pump in Pseudomonas aeruginosa without an anchoring membrane.";
J. Biol. Chem. 275:4628-4634(2000).
[9]
ASSEMBLY OF TRIPARTITE EFFLUX COMPLEX.
STRAIN=PAO4290;
PubMed=15325256; DOI=10.1016/j.bbrc.2004.07.140;
Mokhonov V.V., Mokhonova E.I., Akama H., Nakae T.;
"Role of the membrane fusion protein in the assembly of resistance-
nodulation-cell division multidrug efflux pump in Pseudomonas
aeruginosa.";
Biochem. Biophys. Res. Commun. 322:483-489(2004).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-383.
STRAIN=PAO4290;
PubMed=15117957; DOI=10.1074/jbc.C400164200;
Akama H., Matsuura T., Kashiwagi S., Yoneyama H., Narita S.,
Tsukihara T., Nakagawa A., Nakae T.;
"Crystal structure of the membrane fusion protein, MexA, of the
multidrug transporter in Pseudomonas aeruginosa.";
J. Biol. Chem. 279:25939-25942(2004).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 24-383.
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=15226509; DOI=10.1073/pnas.0400375101;
Higgins M.K., Bokma E., Koronakis E., Hughes C., Koronakis V.;
"Structure of the periplasmic component of a bacterial drug efflux
pump.";
Proc. Natl. Acad. Sci. U.S.A. 101:9994-9999(2004).
-!- FUNCTION: The periplasmic linker 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. Required for assembly of the MexA/MexB/OprM complex.
Implicated in the secretion of the siderophore pyoverdine.
-!- FUNCTION: 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.
-!- SUBUNIT: Component of the MexAB-OprM multidrug efflux complex
composed of an unknown number of MexA subunits, MexB and an OprM
homotrimer. The MexA subunits are thought to form a barrel between
the MexB inner membrane transporter and the trimeric OprM outer
membrane channel protein. The N-terminus of the MexA subunits are
anchored to the inner membrane while the alpha-helices of each
subunit are hypothesized to form the barrel which would allow
substrates to pass directly from the cytoplasm/inner membrane to
the external mileu. How the MexA subunits interact with OprM and
MexB, and how the OprM channel is opened is unknown.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:10671490}; Lipid-anchor {ECO:0000255|PROSITE-
ProRule:PRU00303, ECO:0000269|PubMed:10671490}. Note=The membrane
anchor is not necessary for antibiotic efflux as the protein is
functional when targeted to the periplasm by a foreign signal
peptide.
-!- INDUCTION: By growth under severe iron limitation.
-!- MISCELLANEOUS: In both X-ray crystal structures approximately the
last 100 residues are not ordered.
-!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC
8.A.1) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L11616; AAA74436.1; -; Genomic_DNA.
EMBL; AE004091; AAG03814.1; -; Genomic_DNA.
EMBL; AF092566; AAD45627.1; -; Genomic_DNA.
PIR; S39629; S39629.
RefSeq; NP_249116.1; NC_002516.2.
RefSeq; WP_003118819.1; NC_002516.2.
PDB; 1T5E; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M=24-383.
PDB; 1VF7; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M=25-383.
PDB; 2V4D; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M=24-383.
PDB; 4DK1; X-ray; 3.50 A; A/B/C/D=95-158.
PDBsum; 1T5E; -.
PDBsum; 1VF7; -.
PDBsum; 2V4D; -.
PDBsum; 4DK1; -.
ProteinModelPortal; P52477; -.
SMR; P52477; -.
IntAct; P52477; 1.
STRING; 208964.PA0425; -.
DrugBank; DB04077; Glycerol.
TCDB; 2.A.6.2.6; the resistance-nodulation-cell division (rnd) superfamily.
PaxDb; P52477; -.
PRIDE; P52477; -.
EnsemblBacteria; AAG03814; AAG03814; PA0425.
GeneID; 877855; -.
KEGG; pae:PA0425; -.
PATRIC; fig|208964.12.peg.447; -.
PseudoCAP; PA0425; -.
eggNOG; ENOG4105C1P; Bacteria.
eggNOG; ENOG410XNVN; LUCA.
InParanoid; P52477; -.
KO; K03585; -.
OMA; QLTVKRY; -.
PhylomeDB; P52477; -.
EvolutionaryTrace; P52477; -.
Proteomes; UP000002438; Chromosome.
GO; GO:0031226; C:intrinsic component of plasma membrane; IBA:GO_Central.
GO; GO:0015238; F:drug transmembrane transporter activity; IMP:PseudoCAP.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0051260; P:protein homooligomerization; IMP:CAFA.
GO; GO:0046677; P:response to antibiotic; IDA:PseudoCAP.
InterPro; IPR032317; HlyD_D23.
InterPro; IPR006143; RND_pump_MFP.
Pfam; PF00529; HlyD; 1.
Pfam; PF16576; HlyD_D23; 1.
TIGRFAMs; TIGR01730; RND_mfp; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Cell inner membrane;
Cell membrane; Coiled coil; Complete proteome;
Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal; Transport.
SIGNAL 1 23
CHAIN 24 383 Multidrug resistance protein MexA.
/FTId=PRO_0000018712.
COILED 97 151
LIPID 24 24 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000269|PubMed:10671490}.
LIPID 24 24 S-diacylglycerol cysteine.
{ECO:0000305|PubMed:10671490}.
MUTAGEN 24 24 C->F,Y: No palmitoylation occurs. Some of
the protein becomes soluble, some remains
attached to the inner membrane. The
protein functions normally in antibiotic
efflux. {ECO:0000269|PubMed:10671490}.
CONFLICT 210 210 L -> M (in Ref. 4; AAD45627).
{ECO:0000305}.
STRAND 37 42 {ECO:0000244|PDB:2V4D}.
STRAND 51 57 {ECO:0000244|PDB:1VF7}.
STRAND 59 61 {ECO:0000244|PDB:1VF7}.
STRAND 63 66 {ECO:0000244|PDB:1VF7}.
STRAND 72 76 {ECO:0000244|PDB:1VF7}.
STRAND 81 85 {ECO:0000244|PDB:1VF7}.
STRAND 89 94 {ECO:0000244|PDB:1VF7}.
HELIX 97 125 {ECO:0000244|PDB:1VF7}.
HELIX 131 156 {ECO:0000244|PDB:1VF7}.
STRAND 159 161 {ECO:0000244|PDB:1VF7}.
STRAND 163 168 {ECO:0000244|PDB:1VF7}.
STRAND 187 191 {ECO:0000244|PDB:1VF7}.
STRAND 194 197 {ECO:0000244|PDB:1VF7}.
STRAND 200 203 {ECO:0000244|PDB:1VF7}.
HELIX 204 215 {ECO:0000244|PDB:1VF7}.
STRAND 217 219 {ECO:0000244|PDB:2V4D}.
STRAND 221 223 {ECO:0000244|PDB:1VF7}.
STRAND 226 228 {ECO:0000244|PDB:1VF7}.
STRAND 229 232 {ECO:0000244|PDB:1T5E}.
STRAND 238 241 {ECO:0000244|PDB:1VF7}.
STRAND 244 248 {ECO:0000244|PDB:1VF7}.
STRAND 254 261 {ECO:0000244|PDB:1VF7}.
STRAND 263 266 {ECO:0000244|PDB:1VF7}.
STRAND 268 270 {ECO:0000244|PDB:1VF7}.
STRAND 277 283 {ECO:0000244|PDB:1VF7}.
STRAND 286 289 {ECO:0000244|PDB:1VF7}.
STRAND 292 294 {ECO:0000244|PDB:2V4D}.
HELIX 295 297 {ECO:0000244|PDB:2V4D}.
STRAND 299 301 {ECO:0000244|PDB:2V4D}.
TURN 302 304 {ECO:0000244|PDB:2V4D}.
STRAND 305 311 {ECO:0000244|PDB:2V4D}.
STRAND 315 322 {ECO:0000244|PDB:2V4D}.
STRAND 331 337 {ECO:0000244|PDB:2V4D}.
STRAND 343 347 {ECO:0000244|PDB:2V4D}.
TURN 348 350 {ECO:0000244|PDB:2V4D}.
SEQUENCE 383 AA; 40970 MW; 0D161F917B3529F2 CRC64;
MQRTPAMRVL VPALLVAISA LSGCGKSEAP PPAQTPEVGI VTLEAQTVTL NTELPGRTNA
FRIAEVRPQV NGIILKRLFK EGSDVKAGQQ LYQIDPATYE ADYQSAQANL ASTQEQAQRY
KLLVADQAVS KQQYADANAA YLQSKAAVEQ ARINLRYTKV LSPISGRIGR SAVTEGALVT
NGQANAMATV QQLDPIYVDV TQPSTALLRL RRELASGQLE RAGDNAAKVS LKLEDGSQYP
LEGRLEFSEV SVDEGTGSVT IRAVFPNPNN ELLPGMFVHA QLQEGVKQKA ILAPQQGVTR
DLKGQATALV VNAQNKVELR VIKADRVIGD KWLVTEGLNA GDKIITEGLQ FVQPGVEVKT
VPAKNVASAQ KADAAPAKTD SKG


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