ACRZ_ECOLI
ID ACRZ_ECOLI Reviewed; 49 AA.
AC P0AAW9; P75759;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Multidrug efflux pump accessory protein AcrZ {ECO:0000255|HAMAP-Rule:MF_01484};
DE AltName: Full=AcrAB-TolC multidrug efflux pump accessory protein AcrZ {ECO:0000255|HAMAP-Rule:MF_01484};
DE AltName: Full=Acridine resistance protein Z {ECO:0000255|HAMAP-Rule:MF_01484};
GN Name=acrZ {ECO:0000255|HAMAP-Rule:MF_01484}; Synonyms=ybhT;
GN OrderedLocusNames=b0762, JW5102;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19121005; DOI=10.1111/j.1365-2958.2008.06495.x;
RA Hemm M.R., Paul B.J., Schneider T.D., Storz G., Rudd K.E.;
RT "Small membrane proteins found by comparative genomics and ribosome binding
RT site models.";
RL Mol. Microbiol. 70:1487-1501(2008).
RN [5]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19734316; DOI=10.1128/jb.00872-09;
RA Hemm M.R., Paul B.J., Miranda-Rios J., Zhang A., Soltanzad N., Storz G.;
RT "Small stress response proteins in Escherichia coli: proteins missed by
RT classical proteomic studies.";
RL J. Bacteriol. 192:46-58(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.m111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [7]
RP FUNCTION, INTERACTION WITH ACRB, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-30 AND 46-GLY--HIS-49.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23010927; DOI=10.1073/pnas.1210093109;
RA Hobbs E.C., Yin X., Paul B.J., Astarita J.L., Storz G.;
RT "Conserved small protein associates with the multidrug efflux pump AcrB and
RT differentially affects antibiotic resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16696-16701(2012).
CC -!- FUNCTION: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with a
CC broad substrate specificity. This protein binds to AcrB and is required
CC for efflux of some but not all substrates, suggesting it may influence
CC the specificity of drug export. {ECO:0000255|HAMAP-Rule:MF_01484,
CC ECO:0000269|PubMed:23010927}.
CC -!- SUBUNIT: Part of the AcrA-AcrB-AcrZ-TolC efflux pump, interacts
CC directly with AcrB. {ECO:0000255|HAMAP-Rule:MF_01484,
CC ECO:0000269|PubMed:23010927}.
CC -!- INTERACTION:
CC P0AAW9; P31224: acrB; NbExp=7; IntAct=EBI-6313593, EBI-551006;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01484, ECO:0000269|PubMed:19121005,
CC ECO:0000269|PubMed:21778229}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01484, ECO:0000269|PubMed:19121005,
CC ECO:0000269|PubMed:21778229}. Note=In sucrose cushions fractionates
CC with both the inner and outer membranes.
CC -!- INDUCTION: Constitutively expressed (PubMed:19121005), may be repressed
CC at 45 degrees Celsius (PubMed:19121005) (at protein level). Positively
CC regulated by MarA, Rob and SoxS transcriptional regulators.
CC {ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:19734316,
CC ECO:0000269|PubMed:23010927}.
CC -!- DISRUPTION PHENOTYPE: Becomes sensitive to some antibiotics
CC (chloramphenicol, puromycin and tetracycline) but not to others
CC (erythromycin, rifampicin and fusidic acid).
CC {ECO:0000269|PubMed:23010927}.
CC -!- SIMILARITY: Belongs to the AcrZ family. {ECO:0000255|HAMAP-
CC Rule:MF_01484}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC73849.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35426.2; -; Genomic_DNA.
DR PIR; B64812; B64812.
DR RefSeq; NP_415283.1; NC_000913.3.
DR RefSeq; WP_000891515.1; NZ_STEB01000028.1.
DR PDB; 4C48; X-ray; 3.30 A; C=1-49.
DR PDB; 5NC5; X-ray; 3.20 A; F/G/H=1-49.
DR PDB; 5NG5; EM; 6.50 A; M/N/O=1-49.
DR PDB; 5O66; EM; 5.90 A; M/N/O=1-49.
DR PDB; 6SGR; EM; 3.17 A; F/G/H=1-49.
DR PDBsum; 4C48; -.
DR PDBsum; 5NC5; -.
DR PDBsum; 5NG5; -.
DR PDBsum; 5O66; -.
DR PDBsum; 6SGR; -.
DR AlphaFoldDB; P0AAW9; -.
DR SMR; P0AAW9; -.
DR BioGRID; 4259947; 12.
DR DIP; DIP-11423N; -.
DR IntAct; P0AAW9; 2.
DR STRING; 511145.b0762; -.
DR TCDB; 2.A.6.2.2; the resistance-nodulation-cell division (rnd) superfamily.
DR TCDB; 8.A.50.1.1; the acrz rnd auxiliary subunit (acrz) family.
DR PaxDb; P0AAW9; -.
DR PRIDE; P0AAW9; -.
DR EnsemblBacteria; AAC73849; AAC73849; b0762.
DR EnsemblBacteria; BAA35426; BAA35426; BAA35426.
DR GeneID; 67413801; -.
DR GeneID; 945365; -.
DR KEGG; ecj:JW5102; -.
DR KEGG; eco:b0762; -.
DR PATRIC; fig|1411691.4.peg.1516; -.
DR EchoBASE; EB4074; -.
DR HOGENOM; CLU_196028_0_1_6; -.
DR PhylomeDB; P0AAW9; -.
DR BioCyc; EcoCyc:G6396-MON; -.
DR PRO; PR:P0AAW9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0036460; P:cellular response to cell envelope stress; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR HAMAP; MF_01484; AcrZ; 1.
DR InterPro; IPR019702; AcrZ.
DR Pfam; PF10766; AcrZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..49
FT /note="Multidrug efflux pump accessory protein AcrZ"
FT /id="PRO_0000013811"
FT TOPO_DOM 1..7
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01484"
FT TOPO_DOM 29..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MUTAGEN 30
FT /note="G->R: Loss of chloramphenicol resistance, does not
FT bind AcrB (dominant-negative to wild-type). Partially
FT suppressed by AcrB H526Y."
FT /evidence="ECO:0000269|PubMed:23010927"
FT MUTAGEN 46..49
FT /note="Missing: Loss of chloramphenicol resistance, still
FT binds AcrB (dominant-negative to wild-type)."
FT /evidence="ECO:0000269|PubMed:23010927"
FT HELIX 2..35
FT /evidence="ECO:0007829|PDB:6SGR"
SQ SEQUENCE 49 AA; 5300 MW; 1B1185D27F1F37F7 CRC64;
MLELLKSLVF AVIMVPVVMA IILGLIYGLG EVFNIFSGVG KKDQPGQNH
