YQJA_ECOLI
ID YQJA_ECOLI Reviewed; 220 AA.
AC P0AA63; P42614; Q2M9B1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Inner membrane protein YqjA;
GN Name=yqjA; OrderedLocusNames=b3095, JW3066;
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 / 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Mizobuchi K.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
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).
RN [5]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=16861804; DOI=10.1271/bbb.60024;
RA Yamamoto K., Ishihama A.;
RT "Characterization of copper-inducible promoters regulated by CpxA/CpxR in
RT Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 70:1688-1695(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18456815; DOI=10.1128/jb.00414-08;
RA Thompkins K., Chattopadhyay B., Xiao Y., Henk M.C., Doerrler W.T.;
RT "Temperature sensitivity and cell division defects in an Escherichia coli
RT strain with mutations in yghB and yqjA, encoding related and conserved
RT inner membrane proteins.";
RL J. Bacteriol. 190:4489-4500(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19880597; DOI=10.1128/jb.00716-09;
RA Sikdar R., Doerrler W.T.;
RT "Inefficient Tat-dependent export of periplasmic amidases in an Escherichia
RT coli strain with mutations in two DedA family genes.";
RL J. Bacteriol. 192:807-818(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-39 AND ASP-51.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=24277026; DOI=10.1128/aac.02238-13;
RA Kumar S., Doerrler W.T.;
RT "Members of the conserved DedA family are likely membrane transporters and
RT are required for drug resistance in Escherichia coli.";
RL Antimicrob. Agents Chemother. 58:923-930(2014).
CC -!- FUNCTION: May be a membrane transporter required for proton motive
CC force (PMF)-dependent drug efflux. Required, with YghB, for the proper
CC export of certain periplasmic amidases and, possibly, other Tat
CC substrates. May play a role in determining membrane lipid composition.
CC {ECO:0000269|PubMed:18456815, ECO:0000269|PubMed:19880597,
CC ECO:0000269|PubMed:24277026}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Regulated by the CpxA/CpxR two-component system.
CC {ECO:0000269|PubMed:16861804}.
CC -!- DISRUPTION PHENOTYPE: Double mutants lacking both yghB and yqjA show
CC incomplete cell division, temperature sensitivity and altered
CC phospholipid levels. They are also hypersensitive to several compounds
CC known to be exported by other drug efflux proteins, including ethidium
CC bromide, methyl viologen, acriflavine and beta-lactam antibiotics.
CC Expression of either yghB or yqjA can restore the wild-type phenotype,
CC suggesting that these proteins have redundant functions. Both
CC individual null mutant strains grow normally at all temperatures.
CC {ECO:0000269|PubMed:18456815, ECO:0000269|PubMed:19880597,
CC ECO:0000269|PubMed:24277026}.
CC -!- SIMILARITY: Belongs to the DedA family. {ECO:0000305}.
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DR EMBL; U18997; AAA57899.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76130.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77145.1; -; Genomic_DNA.
DR EMBL; D13328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D65098; D65098.
DR RefSeq; NP_417566.1; NC_000913.3.
DR RefSeq; WP_000422149.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0AA63; -.
DR BioGRID; 4262411; 70.
DR STRING; 511145.b3095; -.
DR TCDB; 9.B.27.2.2; the death effector domain a (deda) family.
DR PaxDb; P0AA63; -.
DR PRIDE; P0AA63; -.
DR EnsemblBacteria; AAC76130; AAC76130; b3095.
DR EnsemblBacteria; BAE77145; BAE77145; BAE77145.
DR GeneID; 67414958; -.
DR GeneID; 947643; -.
DR KEGG; ecj:JW3066; -.
DR KEGG; eco:b3095; -.
DR PATRIC; fig|1411691.4.peg.3633; -.
DR EchoBASE; EB2596; -.
DR eggNOG; COG0586; Bacteria.
DR HOGENOM; CLU_044208_6_2_6; -.
DR InParanoid; P0AA63; -.
DR OMA; SNARFQF; -.
DR PhylomeDB; P0AA63; -.
DR BioCyc; EcoCyc:G7609-MON; -.
DR PRO; PR:P0AA63; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IMP:EcoCyc.
DR InterPro; IPR032818; DedA.
DR InterPro; IPR032816; SNARE_assoc.
DR PANTHER; PTHR30353; PTHR30353; 1.
DR Pfam; PF09335; SNARE_assoc; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..220
FT /note="Inner membrane protein YqjA"
FT /id="PRO_0000161417"
FT TOPO_DOM 1..27
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..191
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 39
FT /note="E->A,Q: Abolishes the ability to restore growth,
FT cell division or drug resistance in double mutant."
FT /evidence="ECO:0000269|PubMed:24277026"
FT MUTAGEN 51
FT /note="D->A,N: Abolishes the ability to restore growth,
FT cell division or drug resistance in double mutant."
FT /evidence="ECO:0000269|PubMed:24277026"
SQ SEQUENCE 220 AA; 24585 MW; 07EE88184D420201 CRC64;
MELLTQLLQA LWAQDFETLA NPSMIGMLYF VLFVILFLEN GLLPAAFLPG DSLLVLVGVL
IAKGAMGYPQ TILLLTVAAS LGCWVSYIQG RWLGNTRTVQ NWLSHLPAHY HQRAHHLFHK
HGLSALLIGR FIAFVRTLLP TIAGLSGLNN ARFQFFNWMS GLLWVLILTT LGYMLGKTPV
FLKYEDQLMS CLMLLPVVLL VFGLAGSLVV LWKKKYGNRG
