ID   NUOK_FRAP2              Reviewed;         105 AA.
AC   B0TWQ4;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Fphi_0939;
OS   Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS   O#319-036).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=484022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25017 / FSC 153 / O#319-036;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Richardson P.;
RT   "Complete sequence of chromosome of Francisella philomiragia subsp.
RT   philomiragia ATCC 25017.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000937; ABZ87162.1; -; Genomic_DNA.
DR   RefSeq; WP_004286961.1; NC_010336.1.
DR   AlphaFoldDB; B0TWQ4; -.
DR   SMR; B0TWQ4; -.
DR   STRING; 484022.Fphi_0939; -.
DR   EnsemblBacteria; ABZ87162; ABZ87162; Fphi_0939.
DR   GeneID; 64050616; -.
DR   KEGG; fph:Fphi_0939; -.
DR   eggNOG; COG0713; Bacteria.
DR   HOGENOM; CLU_144724_2_0_6; -.
DR   OMA; NFVAFSY; -.
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..105
FT                   /note="NADH-quinone oxidoreductase subunit K"
FT                   /id="PRO_0000390063"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
SQ   SEQUENCE   105 AA;  11450 MW;  2A96D0BF56CC874D CRC64;
     MNSISVSVTN GLIFSTLLFV ISVAGIIINR RNILILLMSI ELMLLAVNTN FLIFANMHHQ
     AMGGVFVFFI MAVAAAETAI GLAIVVAIFR KRKTIDLSKL NTLRG