ACRD_ECOLI
ID ACRD_ECOLI Reviewed; 1037 AA.
AC P24177; P76971; P77178; Q46715;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable aminoglycoside efflux pump;
DE AltName: Full=Acriflavine resistance protein D;
GN Name=acrD; Synonyms=yffA; OrderedLocusNames=b2470, JW2454;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nilles M.L., Bertrand K.P.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ma D., Cook D.N., Alberti M., Nikaido H., Hearst J.E.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 998-1037.
RC STRAIN=K12;
RX PubMed=1644752; DOI=10.1128/jb.174.16.5265-5271.1992;
RA Bouvier J., Richaud C., Higgins W., Bogler O., Stragier S.;
RT "Cloning, characterization, and expression of the dapE gene of Escherichia
RT coli.";
RL J. Bacteriol. 174:5265-5271(1992).
RN [7]
RP FUNCTION.
RX PubMed=10692383; DOI=10.1128/jb.182.6.1754-1756.2000;
RA Rosenberg E.Y., Ma D., Nikaido H.;
RT "AcrD of Escherichia coli is an aminoglycoside efflux pump.";
RL J. Bacteriol. 182:1754-1756(2000).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Participates in the efflux of aminoglycosides. Confers
CC resistance to a variety of these substances.
CC {ECO:0000269|PubMed:10692383}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. {ECO:0000305}.
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DR EMBL; U12598; AAA20584.1; -; Genomic_DNA.
DR EMBL; U10436; AAA74741.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75523.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16344.1; -; Genomic_DNA.
DR EMBL; X57403; CAA40663.1; -; Genomic_DNA.
DR PIR; E65022; E65022.
DR RefSeq; NP_416965.1; NC_000913.3.
DR RefSeq; WP_001273151.1; NZ_LN832404.1.
DR AlphaFoldDB; P24177; -.
DR SMR; P24177; -.
DR BioGRID; 4260927; 488.
DR ComplexPortal; CPX-4264; AcrAD-TolC multidrug efflux transport complex.
DR DIP; DIP-9050N; -.
DR IntAct; P24177; 4.
DR STRING; 511145.b2470; -.
DR TCDB; 2.A.6.2.7; the resistance-nodulation-cell division (rnd) superfamily.
DR PaxDb; P24177; -.
DR PRIDE; P24177; -.
DR EnsemblBacteria; AAC75523; AAC75523; b2470.
DR EnsemblBacteria; BAA16344; BAA16344; BAA16344.
DR GeneID; 945464; -.
DR KEGG; ecj:JW2454; -.
DR KEGG; eco:b2470; -.
DR PATRIC; fig|1411691.4.peg.4270; -.
DR EchoBASE; EB0014; -.
DR eggNOG; COG0841; Bacteria.
DR HOGENOM; CLU_002755_0_2_6; -.
DR InParanoid; P24177; -.
DR OMA; FRYNEMG; -.
DR PhylomeDB; P24177; -.
DR BioCyc; EcoCyc:ACRD-MON; -.
DR BioCyc; MetaCyc:ACRD-MON; -.
DR PRO; PR:P24177; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0009636; P:response to toxic substance; IMP:EcoCyc.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IC:ComplexPortal.
DR GO; GO:0042908; P:xenobiotic transport; IDA:EcoCyc.
DR Gene3D; 3.30.2090.10; -; 2.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR004764; HAE1.
DR PANTHER; PTHR32063; PTHR32063; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82714; SSF82714; 2.
DR TIGRFAMs; TIGR00915; 2A0602; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1037
FT /note="Probable aminoglycoside efflux pump"
FT /id="PRO_0000161812"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 29..339
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 340..359
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 360..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 366..385
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 386..391
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 392..413
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 414..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 442..460
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 461..473
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 474..496
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 497..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 538..556
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 557..870
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 871..890
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 891..896
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 897..916
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250"
FT TOPO_DOM 917..922
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 923..944
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 945..971
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 972..990
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250"
FT TOPO_DOM 991..1003
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1004..1026
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1027..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CONFLICT 303
FT /note="A -> G (in Ref. 1; AAA20584)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="V -> E (in Ref. 1; AAA20584)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="A -> D (in Ref. 2; AAA74741)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="G -> P (in Ref. 1; AAA20584)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="S -> PD (in Ref. 1; AAA20584)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="R -> A (in Ref. 1; AAA20584)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="A -> G (in Ref. 1; AAA20584)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="R -> P (in Ref. 1; AAA20584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1037 AA; 113047 MW; 961611E1D24FD4E5 CRC64;
MANFFIDRPI FAWVLAILLC LTGTLAIFSL PVEQYPDLAP PNVRVTANYP GASAQTLENT
VTQVIEQNMT GLDNLMYMSS QSSGTGQASV TLSFKAGTDP DEAVQQVQNQ LQSAMRKLPQ
AVQNQGVTVR KTGDTNILTI AFVSTDGSMD KQDIADYVAS NIQDPLSRVN GVGDIDAYGS
QYSMRIWLDP AKLNSFQMTA KDVTDAIESQ NAQIAVGQLG GTPSVDKQAL NATINAQSLL
QTPEQFRDIT LRVNQDGSEV RLGDVATVEM GAEKYDYLSR FNGKPASGLG VKLASGANEM
ATAELVLNRL DELAQYFPHG LEYKVAYETT SFVKASIEDV VKTLLEAIAL VFLVMYLFLQ
NFRATLIPTI AVPVVLMGTF SVLYAFGYSV NTLTMFAMVL AIGLLVDDAI VVVENVERIM
SEEGLTPREA TRKSMGQIQG ALVGIAMVLS AVFVPMAFFG GTTGAIYRQF SITIVAAMVL
SVLVAMILTP ALCATLLKPL KKGEHHGQKG FFAWFNQMFN RNAERYEKGV AKILHRSLRW
IVIYVLLLGG MVFLFLRLPT SFLPLEDRGM FTTSVQLPSG STQQQTLKVV EQIEKYYFTH
EKDNIMSVFA TVGSGPGGNG QNVARMFIRL KDWSERDSKT GTSFAIIERA TKAFNQIKEA
RVIASSPPAI SGLGSSAGFD MELQDHAGAG HDALMAARNQ LLALAAENPE LTRVRHNGLD
DSPQLQIDID QRKAQALGVA IDDINDTLQT AWGSSYVNDF MDRGRVKKVY VQAAAPYRML
PDDINLWYVR NKDGGMVPFS AFATSRWETG SPRLERYNGY SAVEIVGEAA PGVSTGTAMD
IMESLVKQLP NGFGLEWTAM SYQERLSGAQ APALYAISLL VVFLCLAALY ESWSVPFSVM
LVVPLGVIGA LLATWMRGLE NDVYFQVGLL TVIGLSAKNA ILIVEFANEM NQKGHDLFEA
TLHACRQRLR PILMTSLAFI FGVLPMATST GAGSGGQHAV GTGVMGGMIS ATILAIYFVP
LFFVLVRRRF PLKPRPE
