NUOK_BDEBA
ID NUOK_BDEBA Reviewed; 107 AA.
AC Q6MGN5;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Bd3889;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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; BX842656; CAE81244.1; -; Genomic_DNA.
DR RefSeq; WP_011166187.1; NC_005363.1.
DR AlphaFoldDB; Q6MGN5; -.
DR SMR; Q6MGN5; -.
DR STRING; 264462.Bd3889; -.
DR EnsemblBacteria; CAE81244; CAE81244; Bd3889.
DR KEGG; bba:Bd3889; -.
DR eggNOG; COG0713; Bacteria.
DR HOGENOM; CLU_144724_0_0_7; -.
DR OMA; NFVAFSY; -.
DR OrthoDB; 2081663at2; -.
DR Proteomes; UP000008080; 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;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..107
FT /note="NADH-quinone oxidoreductase subunit K"
FT /id="PRO_0000389957"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TRANSMEM 36..56
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 107 AA; 11894 MW; 731E0F616B24153C CRC64;
MNTEFINNIG LTHYLVLAAL LFVMGMAGVL LRRNVIVLLM SIELMLNSVN LTFVAFSKYL
GLLDGHIMVF FVMTIAAAEA AVGLALAVSI FKRFNEVNIR FFEHLKG