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P44654

- NAPB_HAEIN

UniProt

P44654 - NAPB_HAEIN

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Protein
Periplasmic nitrate reductase, electron transfer subunit
Gene
napB, HI_0347
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - 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)
Binding sitei87 – 871Heme C 1 (covalent)
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)
Binding sitei127 – 1271Heme C 2 (covalent)
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
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: Chromosome

Subcellular locationi

Periplasm 2 Publications

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 Publication
Add
BLAST
Chaini27 – 150124Periplasmic nitrate reductase, electron transfer subunit
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP44654.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the NapB family.

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

« 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: July 9, 2014
This is version 103 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

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