NQRE_NEIMB
ID NQRE_NEIMB Reviewed; 197 AA.
AC Q9K0M7;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
DE Short=Na(+)-NQR subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
DE Short=Na(+)-translocating NQR subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00429};
DE AltName: Full=NQR complex subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
DE AltName: Full=NQR-1 subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
GN Name=nqrE {ECO:0000255|HAMAP-Rule:MF_00429}; OrderedLocusNames=NMB0565;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC ubiquinol by two successive reactions, coupled with the transport of
CC Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are
CC probably involved in the second step, the conversion of ubisemiquinone
CC to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n
CC Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00429};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00429}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00429}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00429}.
CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC Rule:MF_00429}.
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DR EMBL; AE002098; AAF40993.1; -; Genomic_DNA.
DR PIR; H81184; H81184.
DR RefSeq; NP_273609.1; NC_003112.2.
DR RefSeq; WP_002225564.1; NC_003112.2.
DR AlphaFoldDB; Q9K0M7; -.
DR SMR; Q9K0M7; -.
DR STRING; 122586.NMB0565; -.
DR PaxDb; Q9K0M7; -.
DR EnsemblBacteria; AAF40993; AAF40993; NMB0565.
DR KEGG; nme:NMB0565; -.
DR PATRIC; fig|122586.8.peg.724; -.
DR HOGENOM; CLU_095255_0_0_4; -.
DR OMA; MGMCTFL; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00429; NqrE; 1.
DR InterPro; IPR003667; NqrDE/RnfAE.
DR InterPro; IPR010967; NqrE.
DR PANTHER; PTHR30335:SF1; PTHR30335:SF1; 1.
DR Pfam; PF02508; Rnf-Nqr; 1.
DR PIRSF; PIRSF006102; NQR_DE; 1.
DR TIGRFAMs; TIGR01940; nqrE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; NAD;
KW Reference proteome; Sodium; Sodium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..197
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT E"
FT /id="PRO_0000214254"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
SQ SEQUENCE 197 AA; 21179 MW; 768E43B7F8E32326 CRC64;
MEHYLSLFIK SVFIENMALS FFLGMCTFLA VSKKVSTAFG LGVAVIFVLG LSVPVNQLVY
SLLKDGAIAE GVDLTFLKFI TFIGVIAALV QILEMFLDKF VPALYNALGI YLPLITVNCA
IFGAVSFMAQ REYNFGESVV YGFGAGLGWM LAIVALAGIT EKMKYSDAPK GLKGLGITFI
AAGLMAMAFM SFSGIQL
