YGHB_ECOLI
ID YGHB_ECOLI Reviewed; 219 AA.
AC P0AA60; P33196; Q2M9J0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Inner membrane protein YghB;
GN Name=yghB; OrderedLocusNames=b3009, JW2976;
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 1-18.
RX PubMed=3513164; DOI=10.1073/pnas.83.4.867;
RA Belfaiza J., Parsot C., Martel A., de la Tour C.B., Margarita D.,
RA Cohen G.N., Saint-Girons I.;
RT "Evolution in biosynthetic pathways: two enzymes catalyzing consecutive
RT steps in methionine biosynthesis originate from a common ancestor and
RT possess a similar regulatory region.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:867-871(1986).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
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 YqjA, 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 -!- 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; U28377; AAA69176.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76045.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77066.1; -; Genomic_DNA.
DR EMBL; M12858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G65087; G65087.
DR RefSeq; NP_417482.1; NC_000913.3.
DR RefSeq; WP_000268419.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0AA60; -.
DR BioGRID; 4262378; 169.
DR STRING; 511145.b3009; -.
DR TCDB; 9.B.27.2.1; the death effector domain a (deda) family.
DR PaxDb; P0AA60; -.
DR PRIDE; P0AA60; -.
DR EnsemblBacteria; AAC76045; AAC76045; b3009.
DR EnsemblBacteria; BAE77066; BAE77066; BAE77066.
DR GeneID; 58389019; -.
DR GeneID; 947490; -.
DR KEGG; ecj:JW2976; -.
DR KEGG; eco:b3009; -.
DR PATRIC; fig|1411691.4.peg.3721; -.
DR EchoBASE; EB1771; -.
DR eggNOG; COG0586; Bacteria.
DR HOGENOM; CLU_044208_6_2_6; -.
DR InParanoid; P0AA60; -.
DR OMA; FMPLACG; -.
DR PhylomeDB; P0AA60; -.
DR BioCyc; EcoCyc:EG11824-MON; -.
DR PRO; PR:P0AA60; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
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..219
FT /note="Inner membrane protein YghB"
FT /id="PRO_0000161411"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..67
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..191
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 39
FT /note="E->A: Abolishes the ability to restore growth, cell
FT division or drug resistance in double mutant."
FT /evidence="ECO:0000269|PubMed:24277026"
FT MUTAGEN 51
FT /note="D->A: Abolishes the ability to restore growth, cell
FT division or drug resistance in double mutant."
FT /evidence="ECO:0000269|PubMed:24277026"
SQ SEQUENCE 219 AA; 24134 MW; 726BDC4B7194B473 CRC64;
MAVIQDIIAA LWQHDFAALA DPHIVSVVYF VMFATLFLEN GLLPASFLPG DSLLILAGAL
IAQGVMDFLP TIAILTAAAS LGCWLSYIQG RWLGNTKTVK GWLAQLPAKY HQRATCMFDR
HGLLALLAGR FLAFVRTLLP TMAGISGLPN RRFQFFNWLS GLLWVSVVTS FGYALSMIPF
VKRHEDQVMT FLMILPIALL TAGLLGTLFV VIKKKYCNA
