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Multidrug efflux pump subunit AcrA (AcrAB-TolC multidrug efflux pump subunit AcrA) (Acridine resistance protein A)

 ACRA_ECOLI              Reviewed;         397 AA.
P0AE06; P31223; Q2MBW4;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
20-JUN-2018, entry version 113.
RecName: Full=Multidrug efflux pump subunit AcrA;
AltName: Full=AcrAB-TolC multidrug efflux pump subunit AcrA;
AltName: Full=Acridine resistance protein A;
Flags: Precursor;
Name=acrA; Synonyms=lir, mtcA; OrderedLocusNames=b0463, JW0452;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W4573;
PubMed=8407802; DOI=10.1128/jb.175.19.6299-6313.1993;
Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.;
"Molecular cloning and characterization of acrA and acrE genes of
Escherichia coli.";
J. Bacteriol. 175:6299-6313(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Xu J., Bertrand K.P.;
"Nucleotide sequence of the acrAB operon from Escherichia coli.";
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
CHARACTERIZATION.
PubMed=7651136; DOI=10.1111/j.1365-2958.1995.tb02390.x;
Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.;
"Genes acrA and acrB encode a stress-induced efflux system of
Escherichia coli.";
Mol. Microbiol. 16:45-55(1995).
[7]
FUNCTION IN EFFLUX, SUBUNIT, PALMITOYLATION AT CYS-25, AND DISRUPTION
PHENOTYPE.
PubMed=9878415; DOI=10.1006/jmbi.1998.2313;
Zgurskaya H.I., Nikaido H.;
"AcrA is a highly asymmetric protein capable of spanning the
periplasm.";
J. Mol. Biol. 285:409-420(1999).
[8]
PROTEOLYTIC PROCESSING, AND INTERACTION WITH ACRB.
PubMed=10920254; DOI=10.1093/oxfordjournals.jbchem.a022741;
Kawabe T., Fujihira E., Yamaguchi A.;
"Molecular construction of a multidrug exporter system, AcrAB:
molecular interaction between AcrA and AcrB, and cleavage of the N-
terminal signal sequence of AcrA.";
J. Biochem. 128:195-200(2000).
[9]
INTERACTION WITH ACRB AND TOLC, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=15228545; DOI=10.1111/j.1365-2958.2004.04158.x;
Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.;
"Interactions underlying assembly of the Escherichia coli AcrAB-TolC
multidrug efflux system.";
Mol. Microbiol. 53:697-706(2004).
[10]
HOMOTRIMERIZATION, AND SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
PubMed=16079137; DOI=10.1074/jbc.M506479200;
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[11]
SUBUNIT.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=23010927; DOI=10.1073/pnas.1210093109;
Hobbs E.C., Yin X., Paul B.J., Astarita J.L., Storz G.;
"Conserved small protein associates with the multidrug efflux pump
AcrB and differentially affects antibiotic resistance.";
Proc. Natl. Acad. Sci. U.S.A. 109:16696-16701(2012).
[12]
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 45-312, AND MUTAGENESIS OF
223-MET-MET-224 AND 287-LEU-LEU-288.
STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
PubMed=16531241; DOI=10.1016/j.str.2005.11.015;
Mikolosko J., Bobyk K., Zgurskaya H.I., Ghosh P.;
"Conformational flexibility in the multidrug efflux system protein
AcrA.";
Structure 14:577-587(2006).
-!- FUNCTION: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex
with broad substrate specificity that uses the proton motive force
to export substrates. This subunit may act as an adapter protein
that links AcrB and TolC stably together. It is elongated in
shape, being long enough to span the periplasm.
{ECO:0000269|PubMed:9878415}.
-!- SUBUNIT: Monomeric in solution. Homotrimeric; interacts
indpendently with AcrB and TolC as well as AcrZ. Part of the AcrA-
AcrB-TolC efflux pump. Complex assembly is independent of an
efflux substrate and appears to be constitutive.
{ECO:0000269|PubMed:10920254, ECO:0000269|PubMed:15228545,
ECO:0000269|PubMed:23010927, ECO:0000269|PubMed:9878415}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-875601, EBI-875601;
P02930:tolC; NbExp=2; IntAct=EBI-875601, EBI-875614;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137}; Lipid-
anchor {ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137}. Note=An
unlipidated version of this protein (directed to the periplasm by
the OmpA signal sequence) functions normally.
-!- DISRUPTION PHENOTYPE: Cannot grow on efflux substrates novobiocin
or fusidic acid. {ECO:0000269|PubMed:9878415}.
-!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC
8.A.1) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U00734; AAA67134.1; -; Genomic_DNA.
EMBL; M94248; AAA23410.1; -; Genomic_DNA.
EMBL; U82664; AAB40217.1; -; Genomic_DNA.
EMBL; U00096; AAC73565.1; -; Genomic_DNA.
EMBL; AP009048; BAE76242.1; -; Genomic_DNA.
PIR; A36938; A36938.
RefSeq; NP_414996.1; NC_000913.3.
RefSeq; WP_001295324.1; NZ_LN832404.1.
PDB; 2F1M; X-ray; 2.71 A; A/B/C/D=45-312.
PDB; 5NG5; EM; 6.50 A; A/B/D/E/G/H=25-397.
PDB; 5O66; EM; 5.90 A; D/E/F/G/H/I=25-397.
PDB; 5V5S; EM; 6.50 A; D/E/F/G/H/I=1-397.
PDBsum; 2F1M; -.
PDBsum; 5NG5; -.
PDBsum; 5O66; -.
PDBsum; 5V5S; -.
ProteinModelPortal; P0AE06; -.
SMR; P0AE06; -.
BioGrid; 4259860; 404.
DIP; DIP-29039N; -.
IntAct; P0AE06; 5.
STRING; 316385.ECDH10B_0419; -.
TCDB; 8.A.1.6.1; the membrane fusion protein (mfp) family.
EPD; P0AE06; -.
PaxDb; P0AE06; -.
PRIDE; P0AE06; -.
EnsemblBacteria; AAC73565; AAC73565; b0463.
EnsemblBacteria; BAE76242; BAE76242; BAE76242.
GeneID; 945112; -.
KEGG; ecj:JW0452; -.
KEGG; eco:b0463; -.
PATRIC; fig|1411691.4.peg.1813; -.
EchoBASE; EB1654; -.
EcoGene; EG11703; acrA.
eggNOG; ENOG4105C1P; Bacteria.
eggNOG; ENOG410XNVN; LUCA.
HOGENOM; HOG000158247; -.
InParanoid; P0AE06; -.
KO; K03585; -.
OMA; MQFKPAV; -.
PhylomeDB; P0AE06; -.
BioCyc; EcoCyc:EG11703-MONOMER; -.
BioCyc; MetaCyc:EG11703-MONOMER; -.
EvolutionaryTrace; P0AE06; -.
PRO; PR:P0AE06; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:1990281; C:efflux pump complex; IPI:EcoCyc.
GO; GO:0031226; C:intrinsic component of plasma membrane; IBA:GO_Central.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0015238; F:drug transmembrane transporter activity; IMP:EcoliWiki.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0015721; P:bile acid and bile salt transport; IMP:EcoCyc.
GO; GO:0006855; P:drug transmembrane transport; IMP:EcoCyc.
GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
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; Lipoprotein; Membrane;
Palmitate; Reference proteome; Signal; Transport.
SIGNAL 1 24
CHAIN 25 397 Multidrug efflux pump subunit AcrA.
/FTId=PRO_0000018687.
REGION 172 397 Interaction with AcrB.
REGION 313 397 Required for growth on efflux drugs.
COILED 98 172
LIPID 25 25 N-palmitoyl cysteine.
{ECO:0000305|PubMed:9878415}.
LIPID 25 25 S-diacylglycerol cysteine. {ECO:0000305}.
MUTAGEN 1 25 MNKNRGFTPLAVVLMLSGSLALTGC->MKKTAIAIAVALAG
FATVAQA: Fully functional (replaces
endogenous signal and lipid anchor with
periplasmic signal for OmpA).
MUTAGEN 223 224 FL->MM: Wild-type resistance to efflux
substrates. Protein unstable; when
associated with 287-M-M-288.
{ECO:0000269|PubMed:16531241}.
MUTAGEN 287 288 LL->MM: Wild-type resistance to efflux
substrates. Protein unstable; when
associated with 223-M-M-224.
{ECO:0000269|PubMed:16531241}.
STRAND 55 61 {ECO:0000244|PDB:2F1M}.
STRAND 63 68 {ECO:0000244|PDB:2F1M}.
STRAND 74 79 {ECO:0000244|PDB:2F1M}.
STRAND 93 96 {ECO:0000244|PDB:2F1M}.
HELIX 99 130 {ECO:0000244|PDB:2F1M}.
TURN 131 134 {ECO:0000244|PDB:2F1M}.
HELIX 140 172 {ECO:0000244|PDB:2F1M}.
STRAND 182 184 {ECO:0000244|PDB:2F1M}.
STRAND 203 208 {ECO:0000244|PDB:2F1M}.
STRAND 210 219 {ECO:0000244|PDB:2F1M}.
TURN 220 222 {ECO:0000244|PDB:2F1M}.
HELIX 224 230 {ECO:0000244|PDB:2F1M}.
STRAND 244 247 {ECO:0000244|PDB:2F1M}.
STRAND 249 251 {ECO:0000244|PDB:2F1M}.
STRAND 258 263 {ECO:0000244|PDB:2F1M}.
STRAND 269 271 {ECO:0000244|PDB:2F1M}.
STRAND 273 280 {ECO:0000244|PDB:2F1M}.
STRAND 292 297 {ECO:0000244|PDB:2F1M}.
SEQUENCE 397 AA; 42197 MW; 5B81DD5BC2B0A077 CRC64;
MNKNRGFTPL AVVLMLSGSL ALTGCDDKQA QQGGQQMPAV GVVTVKTEPL QITTELPGRT
SAYRIAEVRP QVSGIILKRN FKEGSDIEAG VSLYQIDPAT YQATYDSAKG DLAKAQAAAN
IAQLTVNRYQ KLLGTQYISK QEYDQALADA QQANAAVTAA KAAVETARIN LAYTKVTSPI
SGRIGKSNVT EGALVQNGQA TALATVQQLD PIYVDVTQSS NDFLRLKQEL ANGTLKQENG
KAKVSLITSD GIKFPQDGTL EFSDVTVDQT TGSITLRAIF PNPDHTLLPG MFVRARLEEG
LNPNAILVPQ QGVTRTPRGD ATVLVVGADD KVETRPIVAS QAIGDKWLVT EGLKAGDRVV
ISGLQKVRPG VQVKAQEVTA DNNQQAASGA QPEQSKS


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