NQRE_VIBAL
ID NQRE_VIBAL Reviewed; 198 AA.
AC Q56589; Q56583;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit E {ECO:0000255|HAMAP-Rule:MF_00429, ECO:0000303|PubMed:9490015};
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, ECO:0000269|PubMed:9490015};
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, ECO:0000303|PubMed:7805867};
GN Synonyms=nqr5 {ECO:0000303|PubMed:7729558};
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7729558; DOI=10.1016/0014-5793(95)00283-f;
RA Hayashi M., Hirai K., Unemoto T.;
RT "Sequencing and the alignment of structural genes in the nqr operon
RT encoding the Na(+)-translocating NADH-quinone reductase from Vibrio
RT alginolyticus.";
RL FEBS Lett. 363:75-77(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
RC STRAIN=NCIMB 11038 / LMG 3418;
RX PubMed=7805867; DOI=10.1016/0014-5793(94)01275-x;
RA Beattie P., Tan K., Bourne R.M., Leach D.R.F., Rich P.R., Ward F.B.;
RT "Cloning and sequencing of four structural genes for the Na(+)-
RT translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus.";
RL FEBS Lett. 356:333-338(1994).
RN [3]
RP PROTEIN SEQUENCE OF 1-8, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=9490015; DOI=10.1016/s0014-5793(98)00016-7;
RA Nakayama Y., Hayashi M., Unemoto T.;
RT "Identification of six subunits constituting Na+-translocating NADH-quinone
RT reductase from the marine Vibrio alginolyticus.";
RL FEBS Lett. 422:240-242(1998).
RN [4]
RP INHIBITION OF ENZYMATIC ACTIVITY.
RX PubMed=10549856; DOI=10.1248/bpb.22.1064;
RA Nakayama Y., Hayashi M., Yoshikawa K., Mochida K., Unemoto T.;
RT "Inhibitor studies of a new antibiotic, korormicin, 2-n-heptyl-4-
RT hydroxyquinoline N-oxide and Ag+ toward the Na+-translocating NADH-quinone
RT reductase from the marine Vibrio alginolyticus.";
RL Biol. Pharm. Bull. 22:1064-1067(1999).
RN [5]
RP REVIEW.
RX PubMed=11248187; DOI=10.1016/s0005-2728(00)00275-9;
RA Hayashi M., Nakayama Y., Unemoto T.;
RT "Recent progress in the Na(+)-translocating NADH-quinone reductase from the
RT marine Vibrio alginolyticus.";
RL Biochim. Biophys. Acta 1505:37-44(2001).
RN [6]
RP REVIEW.
RX PubMed=11248188; DOI=10.1016/s0005-2728(00)00276-0;
RA Steuber J.;
RT "Na(+) translocation by bacterial NADH:quinone oxidoreductases: an
RT extension to the complex-I family of primary redox pumps.";
RL Biochim. Biophys. Acta 1505:45-56(2001).
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 ECO:0000305|PubMed:11248187, ECO:0000305|PubMed:11248188}.
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, ECO:0000269|PubMed:9490015};
CC -!- ACTIVITY REGULATION: This reaction is tightly coupled to the Na(+)
CC pumping activity and specifically requires Na(+) for activity.
CC Inhibited by korormicin and 2-N-heptyl-4-hydroxyquinoline N-oxide
CC (HQNO). {ECO:0000269|PubMed:10549856}.
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00429, ECO:0000269|PubMed:9490015}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00429, ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00429}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9490015}.
CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC Rule:MF_00429, ECO:0000305}.
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DR EMBL; AB008030; BAA22914.1; -; Genomic_DNA.
DR EMBL; Z37111; CAA85480.1; -; Genomic_DNA.
DR PIR; S65530; S65530.
DR RefSeq; WP_005380270.1; NZ_WAHT01000008.1.
DR AlphaFoldDB; Q56589; -.
DR SMR; Q56589; -.
DR STRING; 663.BAU10_10820; -.
DR TCDB; 3.D.5.1.1; the na(+)-translocating nadh:quinone dehydrogenase (na-ndh or nqr) family.
DR GeneID; 61533193; -.
DR eggNOG; COG2209; Bacteria.
DR OrthoDB; 1814639at2; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Ion transport; Membrane; NAD; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..198
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT E"
FT /id="PRO_0000214257"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT CONFLICT 13..17
FT /note="FIENM -> SSKH (in Ref. 2; CAA85480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21540 MW; 6173F4DED143E358 CRC64;
MEHYISLLVK SIFIENMALS FFLGMCTFLA VSKKVKTSFG LGVAVVVVLT IAVPVNNLVY
NLVLRENALV EGVDLSFLNF ITFIGVIAAL VQILEMVLDR FFPPLYNALG IFLPLITVNC
AIFGGVSFMV QRDYNFAESI VYGFGSGVGW MLAIVALAGI REKMKYSDVP PGLRGLGITF
ITVGLMALGF MSFSGVQL
