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Protein

Periplasmic nitrate reductase, electron transfer subunit

Gene

napB

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 – 884Combined sources
Turni90 – 923Combined sources
Helixi93 – 964Combined sources
Helixi103 – 1053Combined sources
Helixi124 – 1263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MINMTKQVSK ILAGLFTALF AGSLMASDAP AVGKDLTQAA ENIPPAFHNA
60 70 80 90 100
PRQGELPALN YVNQPPMVPH SVANYQVTKN VNQCLNCHSP ENSRLSGATR
110 120 130 140 150
ISPTHFMDRD GKVGSSSSPR RYFCLQCHVS QANVDPIVPN DFKPMKGYGN
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:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22008.1.
PIRiC64149.
RefSeqiNP_438511.1. NC_000907.1.
WP_005691774.1. NC_000907.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22008.1.
PIRiC64149.
RefSeqiNP_438511.1. NC_000907.1.
WP_005691774.1. NC_000907.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi71421.HI0347.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG3043.
KOiK02568.
OMAiNHIKEST.
OrthoDBiEOG6CGCD3.
PhylomeDBiP44654.

Miscellaneous databases

EvolutionaryTraceiP44654.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.