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C5W716 (NUOK_ECOBD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-quinone oxidoreductase subunit K

EC=1.6.99.5
Alternative name(s):
NADH dehydrogenase I subunit K
NDH-1 subunit K
Gene names
Name:nuoK
Ordered Locus Names:B21_02164, ECBD_1382, ECD_02204
OrganismEscherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]
Taxonomic identifier469008 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient By similarity. HAMAP-Rule MF_01456

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01456

Subunit structure

NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity.

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01456.

Sequence similarities

Belongs to the complex I subunit 4L family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandNAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMQuinone
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processATP synthesis coupled electron transport

Inferred from electronic annotation. Source: InterPro

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNADH dehydrogenase (quinone) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

quinone binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 100100NADH-quinone oxidoreductase subunit K HAMAP-Rule MF_01456
PRO_0000390042

Regions

Transmembrane4 – 2421Helical; Potential
Transmembrane28 – 4821Helical; Potential
Transmembrane60 – 8021Helical; Potential

Secondary structure

.......... 100
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
C5W716 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: CC5AF3946A879383

FASTA10010,845
        10         20         30         40         50         60 
MIPLQHGLIL AAILFVLGLT GLVIRRNLLF MLIGLEIMIN ASALAFVVAG SYWGQTDGQV 

        70         80         90        100 
MYILAISLAA AEASIGLALL LQLHRRRQNL NIDSVSEMRG 

« Hide

References

[1]"Sequencing and gene expression analysis of Escherichia coli BL21."
Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3.
[2]"Complete sequence of Escherichia coli BL21(DE3)."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3.
[3]"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)."
Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.
J. Mol. Biol. 394:644-652(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM946981 Genomic DNA. Translation: CAQ32681.1.
CP001665 Genomic DNA. Translation: ACT28445.1.
CP001509 Genomic DNA. Translation: ACT44026.1.
RefSeqYP_002999943.1. NC_012892.2.
YP_003035630.1. NC_012947.1.
YP_003054797.1. NC_012971.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RKOX-ray3.00G/K1-100[»]
ProteinModelPortalC5W716.
SMRC5W716. Positions 1-100.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59176N.
STRING469008.ECBD_1382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT28445; ACT28445; ECBD_1382.
ACT44026; ACT44026; ECD_02204.
CAQ32681; CAQ32681; B21_02164.
GeneID8114248.
8156286.
8181254.
KEGGebd:ECBD_1382.
ebe:B21_02164.
ebl:ECD_02204.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0713.
HOGENOMHOG000066429.
KOK00340.
OMAADGQIMF.

Family and domain databases

HAMAPMF_01456. NDH1_NuoK.
InterProIPR001133. NADH_UbQ_OxRdtase_chain4L/K.
[Graphical view]
PANTHERPTHR11434. PTHR11434. 1 hit.
PfamPF00420. Oxidored_q2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOK_ECOBD
AccessionPrimary (citable) accession number: C5W716
Secondary accession number(s): C6E9S3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references