NUOK_ECOBD
ID NUOK_ECOBD Reviewed; 100 AA.
AC C5W716; C6E9S3;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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};
GN OrderedLocusNames=B21_02164, ECBD_1382, ECD_02204;
OS Escherichia coli (strain B / BL21-DE3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=469008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RA Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.;
RT "Sequencing and gene expression analysis of Escherichia coli BL21.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT "Complete sequence of Escherichia coli BL21(DE3).";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RX PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052;
RA Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A.,
RA Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B.,
RA Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.;
RT "Genome sequences of Escherichia coli B strains REL606 and BL21(DE3).";
RL J. Mol. Biol. 394:644-652(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 13 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; AM946981; CAQ32681.1; -; Genomic_DNA.
DR EMBL; CP001665; ACT28445.1; -; Genomic_DNA.
DR EMBL; CP001509; ACT44026.1; -; Genomic_DNA.
DR RefSeq; WP_000612644.1; NZ_CP053602.1.
DR PDB; 3RKO; X-ray; 3.00 A; G/K=1-100.
DR PDBsum; 3RKO; -.
DR AlphaFoldDB; C5W716; -.
DR SMR; C5W716; -.
DR DIP; DIP-59176N; -.
DR IntAct; C5W716; 1.
DR STRING; 469008.B21_02164; -.
DR GeneID; 67516046; -.
DR KEGG; ebd:ECBD_1382; -.
DR KEGG; ebe:B21_02164; -.
DR KEGG; ebl:ECD_02204; -.
DR PATRIC; fig|469008.15.peg.2211; -.
DR eggNOG; COG0713; Bacteria.
DR HOGENOM; CLU_144724_0_1_6; -.
DR OMA; NFVAFSY; -.
DR Proteomes; UP000002032; 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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..100
FT /note="NADH-quinone oxidoreductase subunit K"
FT /id="PRO_0000390042"
FT TRANSMEM 4..24
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 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT HELIX 4..24
FT /evidence="ECO:0007829|PDB:3RKO"
FT HELIX 28..52
FT /evidence="ECO:0007829|PDB:3RKO"
FT HELIX 57..82
FT /evidence="ECO:0007829|PDB:3RKO"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:3RKO"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3RKO"
SQ SEQUENCE 100 AA; 10845 MW; CC5AF3946A879383 CRC64;
MIPLQHGLIL AAILFVLGLT GLVIRRNLLF MLIGLEIMIN ASALAFVVAG SYWGQTDGQV
MYILAISLAA AEASIGLALL LQLHRRRQNL NIDSVSEMRG
