Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P44654

- NAPB_HAEIN

UniProt

P44654 - NAPB_HAEIN

Protein

Periplasmic nitrate reductase, electron transfer subunit

Gene

napB

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor.1 Publication

    Redox potential

    E0 are -25 mV and -175 mV.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi70 – 701Iron (heme C 1 axial ligand); via tele nitrogen
    Binding sitei84 – 841Heme C 1 (covalent)1 Publication
    Binding sitei87 – 871Heme C 1 (covalent)1 Publication
    Metal bindingi88 – 881Iron (heme C 1 axial ligand); via tele nitrogen
    Metal bindingi105 – 1051Iron (heme C 2 axial ligand); via tele nitrogen
    Binding sitei124 – 1241Heme C 2 (covalent)1 Publication
    Binding sitei127 – 1271Heme C 2 (covalent)1 Publication
    Metal bindingi128 – 1281Iron (heme C 2 axial ligand); via tele nitrogen

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Periplasmic nitrate reductase, electron transfer subunit
    Alternative name(s):
    Diheme cytochrome c NapB
    Gene namesi
    Name:napB
    Ordered Locus Names:HI_0347
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    Subcellular locationi

    Periplasm 2 Publications

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 150124Periplasmic nitrate reductase, electron transfer subunitPRO_0000006589Add
    BLAST

    Post-translational modificationi

    Binds 2 heme C groups per subunit.

    Interactioni

    Subunit structurei

    Component of the periplasmic nitrate reductase NapAB complex composed of NapA and NapB.By similarity

    Protein-protein interaction databases

    STRINGi71421.HI0347.

    Structurei

    Secondary structure

    1
    150
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi85 – 884
    Turni90 – 923
    Helixi93 – 964
    Helixi103 – 1053
    Helixi124 – 1263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JNIX-ray1.25A28-150[»]
    ProteinModelPortaliP44654.
    SMRiP44654. Positions 64-130.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP44654.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi115 – 1184Poly-Ser

    Sequence similaritiesi

    Belongs to the NapB family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3043.
    KOiK02568.
    OMAiNHIKEST.
    OrthoDBiEOG6CGCD3.
    PhylomeDBiP44654.

    Family and domain databases

    Gene3Di4.10.1020.10. 1 hit.
    InterProiIPR011031. Multihaem_cyt.
    IPR005591. NapB.
    IPR027406. NapB_heme-bd.
    [Graphical view]
    PfamiPF03892. NapB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006105. NapB. 1 hit.
    PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P44654-1 [UniParc]FASTAAdd to Basket

    « Hide

    MINMTKQVSK ILAGLFTALF AGSLMASDAP AVGKDLTQAA ENIPPAFHNA    50
    PRQGELPALN YVNQPPMVPH SVANYQVTKN VNQCLNCHSP ENSRLSGATR 100
    ISPTHFMDRD GKVGSSSSPR RYFCLQCHVS QANVDPIVPN DFKPMKGYGN 150
    Length:150
    Mass (Da):16,255
    Last modified:November 1, 1995 - v1
    Checksum:iC5E98C4E1B29E01F
    GO

    Mass spectrometryi

    Molecular mass is 14748.68 Da from positions 27 - 150. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC22008.1.
    PIRiC64149.
    RefSeqiNP_438511.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC22008; AAC22008; HI_0347.
    GeneIDi949780.
    KEGGihin:HI0347.
    PATRICi20189241. VBIHaeInf48452_0366.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC22008.1 .
    PIRi C64149.
    RefSeqi NP_438511.1. NC_000907.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JNI X-ray 1.25 A 28-150 [» ]
    ProteinModelPortali P44654.
    SMRi P44654. Positions 64-130.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI0347.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC22008 ; AAC22008 ; HI_0347 .
    GeneIDi 949780.
    KEGGi hin:HI0347.
    PATRICi 20189241. VBIHaeInf48452_0366.

    Phylogenomic databases

    eggNOGi COG3043.
    KOi K02568.
    OMAi NHIKEST.
    OrthoDBi EOG6CGCD3.
    PhylomeDBi P44654.

    Miscellaneous databases

    EvolutionaryTracei P44654.

    Family and domain databases

    Gene3Di 4.10.1020.10. 1 hit.
    InterProi IPR011031. Multihaem_cyt.
    IPR005591. NapB.
    IPR027406. NapB_heme-bd.
    [Graphical view ]
    Pfami PF03892. NapB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006105. NapB. 1 hit.
    PROSITEi PS51008. MULTIHEME_CYTC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
    2. "Overproduction, purification and novel redox properties of the dihaem cytochrome c, NapB, from Haemophilus influenzae."
      Brige A., Cole J.A., Hagen W.R., Guisez Y., Van Beeumen J.J.
      Biochem. J. 356:851-858(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-31, FUNCTION, ABSORPTION SPECTROSCOPY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PTM, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
    3. "Crystallization and preliminary X-ray analysis of the recombinant dihaem cytochrome c (NapB) from Haemophilus influenzae."
      Brige A., Leys D., Van Beeumen J.J.
      Acta Crystallogr. D 57:418-420(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
    4. "The 1.25 A resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement."
      Brige A., Leys D., Meyer T.E., Cusanovich M.A., Van Beeumen J.J.
      Biochemistry 41:4827-4836(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 28-150 IN COMPLEX WITH HEME C, PTM.
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

    Entry informationi

    Entry nameiNAPB_HAEIN
    AccessioniPrimary (citable) accession number: P44654
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3