ID   NUOK_BLOPB              Reviewed;         100 AA.
AC   Q492I5;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=BPEN_500;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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 13 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; CP000016; AAZ41114.1; -; Genomic_DNA.
DR   RefSeq; WP_011283025.1; NC_007292.1.
DR   AlphaFoldDB; Q492I5; -.
DR   SMR; Q492I5; -.
DR   STRING; 291272.BPEN_500; -.
DR   EnsemblBacteria; AAZ41114; AAZ41114; BPEN_500.
DR   KEGG; bpn:BPEN_500; -.
DR   eggNOG; COG0713; Bacteria.
DR   HOGENOM; CLU_144724_0_1_6; -.
DR   OMA; NFVAFSY; -.
DR   Proteomes; UP000007794; 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 inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..100
FT                   /note="NADH-quinone oxidoreductase subunit K"
FT                   /id="PRO_0000389961"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
SQ   SEQUENCE   100 AA;  11001 MW;  C4693D13A8606760 CRC64;
     MIPLSHAFSL SIILFILGLI AIIVRRDLLF ILLGLEIMIN AAASAFVIVG SFLGQSDGQI
     MYILVITLSA SESAVSLALL LQLYRRYHTL HIDNISEMRG