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Q9K0M5

- NQRC_NEIMB

UniProt

Q9K0M5 - NQRC_NEIMB

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
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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

    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-SubCell

    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

    MAKKFDKDSF SGTLIVVLAV SLICSVIVAG AVVGLKPIQE KQKLQDKQGY    50
    ILSVAGLMDK DTDIGKTFAE RIEQRVVDLA TGEYVADAPK DFSARIAGKD 100
    PAQSIRIKTE DDLAGIKSRA KYTEVYLVKG EDGKIGQIIL PMHGNGLWSV 150
    MYGFVAIQPD GNTINGITYY EQGETPGLGG EIGNPLWQQK FVGKKLFDGQ 200
    GKLALHVGKG AGSDKEHGVD ALSGASLTSK GVQGSFAYWF GENGYIPYLN 250
    KLKSAGAQ 258
    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 1, 2014
    This is version 88 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