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Q9K0M5 (NQRC_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Na(+)-translocating NADH-quinone reductase subunit C

Short name=Na(+)-NQR subunit C
Short name=Na(+)-translocating NQR subunit C
EC=1.6.5.-
Alternative name(s):
NQR complex subunit C
NQR-1 subunit C
Gene names
Name:nqrC
Ordered Locus Names:NMB0567
OrganismNeisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]
Taxonomic identifier122586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na+ ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol By similarity. HAMAP-Rule MF_00427

Catalytic activity

NADH + ubiquinone + Na+(In) = NAD+ + ubiquinol + Na+(Out). HAMAP-Rule MF_00427

Cofactor

FMN By similarity. HAMAP-Rule MF_00427

Subunit structure

Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and NqrF By similarity.

Subcellular location

Cell inner membrane Potential HAMAP-Rule MF_00427.

Sequence similarities

Belongs to the NqrC family.

Caution

The residue potentially involved in the covalent binding of FMN is a Ser instead of a Thr.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Na(+)-translocating NADH-quinone reductase subunit C HAMAP-Rule MF_00427
PRO_0000214218

Regions

Transmembrane13 – 3523Helical; Potential

Amino acid modifications

Modified residue2261FMN phosphoryl serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K0M5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1F20D8EF011F7C3E

FASTA25827,607
        10         20         30         40         50         60 
MAKKFDKDSF SGTLIVVLAV SLICSVIVAG AVVGLKPIQE KQKLQDKQGY ILSVAGLMDK 

        70         80         90        100        110        120 
DTDIGKTFAE RIEQRVVDLA TGEYVADAPK DFSARIAGKD PAQSIRIKTE DDLAGIKSRA 

       130        140        150        160        170        180 
KYTEVYLVKG EDGKIGQIIL PMHGNGLWSV MYGFVAIQPD GNTINGITYY EQGETPGLGG 

       190        200        210        220        230        240 
EIGNPLWQQK FVGKKLFDGQ GKLALHVGKG AGSDKEHGVD ALSGASLTSK GVQGSFAYWF 

       250 
GENGYIPYLN KLKSAGAQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002098 Genomic DNA. Translation: AAF40995.1.
PIRB81185.
RefSeqNP_273611.1. NC_003112.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122586.NMB0567.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF40995; AAF40995; NMB0567.
GeneID902682.
KEGGnme:NMB0567.
PATRIC20356413. VBINeiMen85645_0726.

Phylogenomic databases

eggNOGCOG2869.
HOGENOMHOG000273678.
KOK00348.
OMAKGYGLWS.
OrthoDBEOG6F2981.

Enzyme and pathway databases

BioCycNMEN122586:GHGG-593-MONOMER.

Family and domain databases

HAMAPMF_00427. NqrC.
InterProIPR007329. FMN-bd.
IPR010204. NADH_UbQ_OxRdtase_suC.
[Graphical view]
PfamPF04205. FMN_bind. 1 hit.
[Graphical view]
PIRSFPIRSF009437. NQR-1_subunit_C. 1 hit.
SMARTSM00900. FMN_bind. 1 hit.
[Graphical view]
TIGRFAMsTIGR01938. nqrC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNQRC_NEIMB
AccessionPrimary (citable) accession number: Q9K0M5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 87 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