Periplasmic nitrate reductase, electron transfer subunit precursor - Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

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P44654 (NAPB_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Periplasmic nitrate reductase, electron transfer subunit

Alternative name(s):
Diheme cytochrome c NapB

Gene names

Name:	napB
Ordered Locus Names:	HI_0347

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

Protein attributes

Sequence length	150 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

Ref.2

Chain

27 – 150

124

Periplasmic nitrate reductase, electron transfer subunit

PRO_0000006589

Regions

Compositional bias

115 – 118

Poly-Ser

Sites

Metal binding

Iron (heme C 1 axial ligand); via tele nitrogen

Metal binding

Iron (heme C 1 axial ligand); via tele nitrogen

Metal binding

105

Iron (heme C 2 axial ligand); via tele nitrogen

Metal binding

128

Iron (heme C 2 axial ligand); via tele nitrogen

Binding site

Heme C 1 (covalent)

Binding site

Heme C 1 (covalent)

Binding site

124

Heme C 2 (covalent)

Binding site

127

Heme C 2 (covalent)

Secondary structure

150

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P44654 [UniParc].

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

FASTA

150

16,255

        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' referencesShow '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. 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, 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.

PIR

C64149.

RefSeq

NP_438511.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JNI	X-ray	1.25	A	28-150	[»]

ProteinModelPortal

P44654.

SMR

P44654. Positions 64-130.

ModBase

Search...

Protein-protein interaction databases

STRING

71421.HI0347.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC22008; AAC22008; HI_0347.

GeneID

949780.

KEGG

hin:HI0347.

PATRIC

20189241. VBIHaeInf48452_0366.

Phylogenomic databases

eggNOG

COG3043.

K02568.

OMA

GNIPTTF.

ProtClustDB

CLSK789811.

Family and domain databases

InterPro

IPR011031. Multihaem_cyt.
IPR005591. NapB.
[Graphical view]

Pfam

PF03892. NapB. 1 hit.
[Graphical view]

PIRSF

PIRSF006105. NapB. 1 hit.

PROSITE

PS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P44654.

Entry information

Entry name

NAPB_HAEIN

Accession

Primary (citable) accession number: P44654

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents