ID   NUOK_BACCQ              Reviewed;         104 AA.
AC   B9IRS5;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=NADH-quinone oxidoreductase subunit K {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 {ECO:0000255|HAMAP-Rule:MF_01456};
DE   AltName: Full=NDH-1 subunit K {ECO:0000255|HAMAP-Rule:MF_01456};
GN   Name=nuoK {ECO:0000255|HAMAP-Rule:MF_01456}; OrderedLocusNames=BCQ_5133;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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 a
CC       menaquinone. 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 membrane {ECO:0000255|HAMAP-Rule:MF_01456};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; CP000227; ACM15533.1; -; Genomic_DNA.
DR   RefSeq; WP_000100082.1; NC_011969.1.
DR   AlphaFoldDB; B9IRS5; -.
DR   SMR; B9IRS5; -.
DR   EnsemblBacteria; ACM15533; ACM15533; BCQ_5133.
DR   GeneID; 64200682; -.
DR   KEGG; bcq:BCQ_5133; -.
DR   HOGENOM; CLU_144724_0_0_9; -.
DR   OMA; NFVAFSY; -.
DR   Proteomes; UP000000441; Chromosome.
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:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
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 membrane; Membrane; NAD; Quinone; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..104
FT                   /note="NADH-quinone oxidoreductase subunit K"
FT                   /id="PRO_0000389947"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
SQ   SEQUENCE   104 AA;  11046 MW;  5A9672243E3B5903 CRC64;
     MSSVPASAYL TLAIILFCIG LFGALTKRNT VIVLVCIELM LNAANLNLVA FSKLGLFPNV
     TGQIFSLFTM AVAAAEAAVG LAILIALYRN RTTVHVDEMD TLKG