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NQRE_AZOVD
ID   NQRE_AZOVD              Reviewed;         202 AA.
AC   C1DR06;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Avin_14630;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/jb.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
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; CP001157; ACO77679.1; -; Genomic_DNA.
DR   RefSeq; WP_012700098.1; NC_012560.1.
DR   AlphaFoldDB; C1DR06; -.
DR   SMR; C1DR06; -.
DR   STRING; 322710.Avin_14630; -.
DR   EnsemblBacteria; ACO77679; ACO77679; Avin_14630.
DR   KEGG; avn:Avin_14630; -.
DR   eggNOG; COG2209; Bacteria.
DR   HOGENOM; CLU_095255_0_0_6; -.
DR   OMA; YFLGMCS; -.
DR   OrthoDB; 1814639at2; -.
DR   Proteomes; UP000002424; 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; IEA:UniProtKB-SubCell.
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; Sodium;
KW   Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..202
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   E"
FT                   /id="PRO_1000206065"
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        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
SQ   SEQUENCE   202 AA;  21827 MW;  5C8D1D48E3CAD414 CRC64;
     MEHYISLFVK SVFIENMALA FFLGMCTFIA ISKKVETAIG LGIAVVVVQA ITVPANNLLY
     AYLLKEGALA WAGLPDIDLS FLGFLSYIGV IAAIVQILEM LLDKYVPSLY NALGIYLPLI
     TVNCAIMAGS LFMVERDYNF PESVVYGIGS GFSWALAIAL LAGIREKLKY SDVPEGLQGL
     GIAFITIGLM SLGFMSFSGI QL
 
 
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