NUOK2_AQUAE
ID NUOK2_AQUAE Reviewed; 102 AA.
AC O67388;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NADH-quinone oxidoreductase subunit K 2 {ECO:0000255|HAMAP-Rule:MF_01456};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NADH dehydrogenase I subunit K 2 {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NDH-1 subunit K 2 {ECO:0000255|HAMAP-Rule:MF_01456};
GN Name=nuoK2 {ECO:0000255|HAMAP-Rule:MF_01456}; OrderedLocusNames=aq_1378;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01456}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01456};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC {ECO:0000255|HAMAP-Rule:MF_01456}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01456}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01456}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4L family.
CC {ECO:0000255|HAMAP-Rule:MF_01456}.
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DR EMBL; AE000657; AAC07351.1; -; Genomic_DNA.
DR PIR; A70420; A70420.
DR RefSeq; NP_213952.1; NC_000918.1.
DR RefSeq; WP_010880890.1; NC_000918.1.
DR AlphaFoldDB; O67388; -.
DR SMR; O67388; -.
DR STRING; 224324.aq_1378; -.
DR EnsemblBacteria; AAC07351; AAC07351; aq_1378.
DR KEGG; aae:aq_1378; -.
DR PATRIC; fig|224324.8.peg.1079; -.
DR eggNOG; COG0713; Bacteria.
DR HOGENOM; CLU_144724_1_1_0; -.
DR InParanoid; O67388; -.
DR OMA; FDVWLSR; -.
DR OrthoDB; 2036866at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_01456; NDH1_NuoK; 1.
DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR InterPro; IPR039428; NUOK/Mnh_C1-like.
DR PANTHER; PTHR11434; PTHR11434; 1.
DR Pfam; PF00420; Oxidored_q2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..102
FT /note="NADH-quinone oxidoreductase subunit K 2"
FT /id="PRO_0000389931"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
SQ SEQUENCE 102 AA; 10905 MW; CCE6159F4CC4A7F4 CRC64;
MKTIPLEAFL TVSMILFGLG LIGIIARRNL VTVLMSLELA LNAVNIALVG ADHYLGLAEG
QIFALFIIAL AATEAAVGLG IIIAIFRLKK VESTDEIREL RG