ID   NUOK2_SOLUE             Reviewed;         102 AA.
AC   Q01UN6;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Acid_5687;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteria; Bryobacterales; Solibacteraceae;
OC   Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(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
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; CP000473; ABJ86634.1; -; Genomic_DNA.
DR   RefSeq; WP_011687369.1; NC_008536.1.
DR   AlphaFoldDB; Q01UN6; -.
DR   SMR; Q01UN6; -.
DR   STRING; 234267.Acid_5687; -.
DR   EnsemblBacteria; ABJ86634; ABJ86634; Acid_5687.
DR   KEGG; sus:Acid_5687; -.
DR   eggNOG; COG0713; Bacteria.
DR   HOGENOM; CLU_144724_0_0_0; -.
DR   OMA; MMLIGIE; -.
DR   OrthoDB; 2081663at2; -.
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..102
FT                   /note="NADH-quinone oxidoreductase subunit K 2"
FT                   /id="PRO_0000390245"
FT   TRANSMEM        4..24
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        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
SQ   SEQUENCE   102 AA;  11083 MW;  C0AE0B74D07A59AE CRC64;
     MHPITPVHYL ALSAALLLIG TVGVLTRRNI VIILMSIELI LNAVNINLIA FSHALQNING
     QIFAIFVITD AVAEAAVGLG ILIALFRNKE TVQADEIDLL KW