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P44654 (NAPB_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Periplasmic nitrate reductase, electron transfer subunit
Alternative name(s):
Diheme cytochrome c NapB
Gene names
Name:napB
Ordered Locus Names:HI_0347
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Subunit structure

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

Subcellular location

Periplasm Ref.2 Ref.3.

Post-translational modification

Binds 2 heme C groups per subunit.

Sequence similarities

Belongs to the NapB family.

Biophysicochemical properties

Redox potential:

E0 are -25 mV and -175 mV. Ref.2

Mass spectrometry

Molecular mass is 14748.68 Da from positions 27 - 150. Determined by ESI. Ref.3

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processoxidation-reduction process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2
Chain27 – 150124Periplasmic nitrate reductase, electron transfer subunit
PRO_0000006589

Regions

Compositional bias115 – 1184Poly-Ser

Sites

Metal binding701Iron (heme C 1 axial ligand); via tele nitrogen
Metal binding881Iron (heme C 1 axial ligand); via tele nitrogen
Metal binding1051Iron (heme C 2 axial ligand); via tele nitrogen
Metal binding1281Iron (heme C 2 axial ligand); via tele nitrogen
Binding site841Heme C 1 (covalent)
Binding site871Heme C 1 (covalent)
Binding site1241Heme C 2 (covalent)
Binding site1271Heme C 2 (covalent)

Secondary structure

.......... 150
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P44654 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C5E98C4E1B29E01F

FASTA15016,255
        10         20         30         40         50         60 
MINMTKQVSK ILAGLFTALF AGSLMASDAP AVGKDLTQAA ENIPPAFHNA PRQGELPALN 

        70         80         90        100        110        120 
YVNQPPMVPH SVANYQVTKN VNQCLNCHSP ENSRLSGATR ISPTHFMDRD GKVGSSSSPR 

       130        140        150 
RYFCLQCHVS QANVDPIVPN DFKPMKGYGN 

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22008.1.
PIRC64149.
RefSeqNP_438511.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNIX-ray1.25A28-150[»]
ProteinModelPortalP44654.
SMRP44654. Positions 64-130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0347.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22008; AAC22008; HI_0347.
GeneID949780.
KEGGhin:HI0347.
PATRIC20189241. VBIHaeInf48452_0366.

Phylogenomic databases

eggNOGCOG3043.
KOK02568.
OMAGNIPTTF.
OrthoDBEOG6CGCD3.
ProtClustDBCLSK789811.

Family and domain databases

Gene3D4.10.1020.10. 1 hit.
InterProIPR011031. Multihaem_cyt.
IPR005591. NapB.
IPR027406. NapB_heme-bd.
[Graphical view]
PfamPF03892. NapB. 1 hit.
[Graphical view]
PIRSFPIRSF006105. NapB. 1 hit.
PROSITEPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP44654.

Entry information

Entry nameNAPB_HAEIN
AccessionPrimary (citable) accession number: P44654
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 101 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names