NUOK_SALTO
ID NUOK_SALTO Reviewed; 105 AA.
AC A4XC28;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Strop_4055;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP56485.1; -; Genomic_DNA.
DR RefSeq; WP_012015253.1; NC_009380.1.
DR AlphaFoldDB; A4XC28; -.
DR SMR; A4XC28; -.
DR STRING; 369723.Strop_4055; -.
DR EnsemblBacteria; ABP56485; ABP56485; Strop_4055.
DR KEGG; stp:Strop_4055; -.
DR PATRIC; fig|369723.5.peg.4193; -.
DR eggNOG; COG0713; Bacteria.
DR HOGENOM; CLU_144724_0_0_11; -.
DR OMA; NFVAFSY; -.
DR Proteomes; UP000000235; 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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..105
FT /note="NADH-quinone oxidoreductase subunit K"
FT /id="PRO_0000390218"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TRANSMEM 34..54
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; 11511 MW; 0B3D4BF4D6ACBB09 CRC64;
MNEFFSVEPN YYLVLAAVLF TIGAAGVLVR RNAIVLFMCV ELMLNAANLT LVTFSRINGD
LNGQIMAFFV MVVAAAEVVV GLAIIMAIYR TRRSASVDDA NLLKY