ID   NUOK2_STRGG             Reviewed;         148 AA.
AC   B1W4V4;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=SGR_2919;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG19748.1; -; Genomic_DNA.
DR   RefSeq; WP_003967022.1; NC_010572.1.
DR   AlphaFoldDB; B1W4V4; -.
DR   SMR; B1W4V4; -.
DR   STRING; 455632.SGR_2919; -.
DR   EnsemblBacteria; BAG19748; BAG19748; SGR_2919.
DR   GeneID; 6209693; -.
DR   KEGG; sgr:SGR_2919; -.
DR   eggNOG; COG0713; Bacteria.
DR   HOGENOM; CLU_144724_1_0_11; -.
DR   OMA; NAITMLM; -.
DR   OrthoDB; 2081663at2; -.
DR   Proteomes; UP000001685; 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..148
FT                   /note="NADH-quinone oxidoreductase subunit K 2"
FT                   /id="PRO_0000390253"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT   REGION          96..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   148 AA;  15420 MW;  ECDF1BB69DA2B148 CRC64;
     MHLAYPAVLA ALLFCVGLYG VLARRNAILV LMSVELMLNA VNLNLVAFDV WLRDTLHSGQ
     ALTLFTIAIA AAEIGIGLAI VLAVYRNRGT SAIDRLRDTA ETDAAETLPD DAGTGPSGTD
     AAPNGDTTTA TGRPGDNAGK NKKAEATR