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Q9K0M5

- NQRC_NEIMB

UniProt

Q9K0M5 - NQRC_NEIMB

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Protein

Na(+)-translocating NADH-quinone reductase subunit C

Gene

nqrC

Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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.By similarity

Catalytic activityi

NADH + ubiquinone + Na+(In) = NAD+ + ubiquinol + Na+(Out).

Cofactori

FMN.By similarity

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB-HAMAP

GO - Biological processi

  1. sodium ion transport Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

Flavoprotein, FMN, NAD, Sodium, Ubiquinone

Enzyme and pathway databases

BioCyciNMEN122586:GHGG-593-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Na(+)-translocating NADH-quinone reductase subunit C (EC:1.6.5.-)
Short name:
Na(+)-NQR subunit C
Short name:
Na(+)-translocating NQR subunit C
Alternative name(s):
NQR complex subunit C
NQR-1 subunit C
Gene namesi
Name:nqrC
Ordered Locus Names:NMB0567
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000425: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. Gram-negative-bacterium-type cell wall Source: InterPro
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Na(+)-translocating NADH-quinone reductase subunit CPRO_0000214218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei226 – 2261FMN phosphoryl serineBy similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi122586.NMB0567.

Structurei

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3523HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the NqrC family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2869.
HOGENOMiHOG000273678.
KOiK00348.
OMAiKGYGLWS.
OrthoDBiEOG6F2981.

Family and domain databases

HAMAPiMF_00427. NqrC.
InterProiIPR007329. FMN-bd.
IPR010204. NADH_UbQ_OxRdtase_suC.
[Graphical view]
PfamiPF04205. FMN_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF009437. NQR-1_subunit_C. 1 hit.
SMARTiSM00900. FMN_bind. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01938. nqrC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9K0M5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKKFDKDSF SGTLIVVLAV SLICSVIVAG AVVGLKPIQE KQKLQDKQGY
60 70 80 90 100
ILSVAGLMDK DTDIGKTFAE RIEQRVVDLA TGEYVADAPK DFSARIAGKD
110 120 130 140 150
PAQSIRIKTE DDLAGIKSRA KYTEVYLVKG EDGKIGQIIL PMHGNGLWSV
160 170 180 190 200
MYGFVAIQPD GNTINGITYY EQGETPGLGG EIGNPLWQQK FVGKKLFDGQ
210 220 230 240 250
GKLALHVGKG AGSDKEHGVD ALSGASLTSK GVQGSFAYWF GENGYIPYLN

KLKSAGAQ
Length:258
Mass (Da):27,607
Last modified:October 1, 2000 - v1
Checksum:i1F20D8EF011F7C3E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002098 Genomic DNA. Translation: AAF40995.1.
PIRiB81185.
RefSeqiNP_273611.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF40995; AAF40995; NMB0567.
GeneIDi902682.
KEGGinme:NMB0567.
PATRICi20356413. VBINeiMen85645_0726.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002098 Genomic DNA. Translation: AAF40995.1 .
PIRi B81185.
RefSeqi NP_273611.1. NC_003112.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 122586.NMB0567.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF40995 ; AAF40995 ; NMB0567 .
GeneIDi 902682.
KEGGi nme:NMB0567.
PATRICi 20356413. VBINeiMen85645_0726.

Phylogenomic databases

eggNOGi COG2869.
HOGENOMi HOG000273678.
KOi K00348.
OMAi KGYGLWS.
OrthoDBi EOG6F2981.

Enzyme and pathway databases

BioCyci NMEN122586:GHGG-593-MONOMER.

Family and domain databases

HAMAPi MF_00427. NqrC.
InterProi IPR007329. FMN-bd.
IPR010204. NADH_UbQ_OxRdtase_suC.
[Graphical view ]
Pfami PF04205. FMN_bind. 1 hit.
[Graphical view ]
PIRSFi PIRSF009437. NQR-1_subunit_C. 1 hit.
SMARTi SM00900. FMN_bind. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01938. nqrC. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC58.

Entry informationi

Entry nameiNQRC_NEIMB
AccessioniPrimary (citable) accession number: Q9K0M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3