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Protein

Nitrate reductase molybdenum cofactor assembly chaperone NarJ

Gene

narJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with the NarI subunit on the membrane.4 Publications

GO - Molecular functioni

  • metallochaperone activity Source: EcoCyc

GO - Biological processi

  • chaperone-mediated protein complex assembly Source: UniProtKB
  • nitrate assimilation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Nitrate assimilation

Enzyme and pathway databases

BioCyciEcoCyc:NARJ-MONOMER.
ECOL316407:JW1217-MONOMER.
BRENDAi1.7.5.1. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase molybdenum cofactor assembly chaperone NarJ
Alternative name(s):
Redox enzyme maturation protein NarJ
Gene namesi
Name:narJ
Ordered Locus Names:b1226, JW1217
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10641. narJ.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Nitrate reductase molybdenum cofactor assembly chaperone NarJPRO_0000096725Add
BLAST

Proteomic databases

PaxDbiP0AF26.
PRIDEiP0AF26.

Interactioni

Subunit structurei

Binds specifically to the NarG subunit of the apoenzyme complex at two distinct sites, one interfering with membrane anchoring and another being involved in molybdenum insertion.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
narGP0915216EBI-555043,EBI-547248
narZP193193EBI-555043,EBI-547262

Protein-protein interaction databases

BioGridi4262232. 7 interactions.
DIPiDIP-35943N.
IntActiP0AF26. 11 interactions.
MINTiMINT-1243008.
STRINGi511145.b1226.

Structurei

3D structure databases

ProteinModelPortaliP0AF26.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NarJ/NarW family.Curated

Phylogenomic databases

eggNOGiENOG4105R3A. Bacteria.
COG2180. LUCA.
HOGENOMiHOG000237365.
InParanoidiP0AF26.
KOiK00373.
OMAiCELFDRG.
OrthoDBiEOG647TXD.
PhylomeDBiP0AF26.

Family and domain databases

Gene3Di1.10.3480.10. 1 hit.
InterProiIPR020945. DMSO/NO3_reduct_chaperone.
IPR003765. NO3_reductase_chaperone_NarJ.
[Graphical view]
PfamiPF02613. Nitrate_red_del. 1 hit.
[Graphical view]
SUPFAMiSSF89155. SSF89155. 1 hit.
TIGRFAMsiTIGR00684. narJ. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AF26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIELVIVSRL LEYPDAALWQ HQQEMFEAIA ASKNLPKEDA HALGIFLRDL
60 70 80 90 100
TTMDPLDAQA QYSELFDRGR ATSLLLFEHV HGESRDRGQA MVDLLAQYEQ
110 120 130 140 150
HGLQLNSREL PDHLPLYLEY LAQLPQSEAV EGLKDIAPIL ALLSARLQQR
160 170 180 190 200
ESRYAVLFDL LLKLANTAID SDKVAEKIAD EARDDTPQAL DAVWEEEQVK
210 220 230
FFADKGCGDS AITAHQRRFA GAVAPQYLNI TTGGQH
Length:236
Mass (Da):26,449
Last modified:December 20, 2005 - v1
Checksum:i17306C34A57DF1E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20147 Genomic DNA. Translation: AAA24196.1.
U00096 Genomic DNA. Translation: AAC74310.1.
AP009048 Genomic DNA. Translation: BAA36096.1.
X16181 Genomic DNA. Translation: CAA34305.1.
PIRiB27737. BVECJ.
RefSeqiNP_415744.1. NC_000913.3.
WP_000571681.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74310; AAC74310; b1226.
BAA36096; BAA36096; BAA36096.
GeneIDi945807.
KEGGiecj:JW1217.
eco:b1226.
PATRICi32117712. VBIEscCol129921_1278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20147 Genomic DNA. Translation: AAA24196.1.
U00096 Genomic DNA. Translation: AAC74310.1.
AP009048 Genomic DNA. Translation: BAA36096.1.
X16181 Genomic DNA. Translation: CAA34305.1.
PIRiB27737. BVECJ.
RefSeqiNP_415744.1. NC_000913.3.
WP_000571681.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AF26.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262232. 7 interactions.
DIPiDIP-35943N.
IntActiP0AF26. 11 interactions.
MINTiMINT-1243008.
STRINGi511145.b1226.

Proteomic databases

PaxDbiP0AF26.
PRIDEiP0AF26.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74310; AAC74310; b1226.
BAA36096; BAA36096; BAA36096.
GeneIDi945807.
KEGGiecj:JW1217.
eco:b1226.
PATRICi32117712. VBIEscCol129921_1278.

Organism-specific databases

EchoBASEiEB0635.
EcoGeneiEG10641. narJ.

Phylogenomic databases

eggNOGiENOG4105R3A. Bacteria.
COG2180. LUCA.
HOGENOMiHOG000237365.
InParanoidiP0AF26.
KOiK00373.
OMAiCELFDRG.
OrthoDBiEOG647TXD.
PhylomeDBiP0AF26.

Enzyme and pathway databases

BioCyciEcoCyc:NARJ-MONOMER.
ECOL316407:JW1217-MONOMER.
BRENDAi1.7.5.1. 2026.

Miscellaneous databases

PROiP0AF26.

Family and domain databases

Gene3Di1.10.3480.10. 1 hit.
InterProiIPR020945. DMSO/NO3_reduct_chaperone.
IPR003765. NO3_reductase_chaperone_NarJ.
[Graphical view]
PfamiPF02613. Nitrate_red_del. 1 hit.
[Graphical view]
SUPFAMiSSF89155. SSF89155. 1 hit.
TIGRFAMsiTIGR00684. narJ. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes."
    Sodergren E.J., Demoss J.A.
    J. Bacteriol. 170:1721-1729(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer."
    Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.
    Mol. Gen. Genet. 218:249-256(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
    Strain: K12 / TG1.
  6. "The narJ gene product is required for biogenesis of respiratory nitrate reductase in Escherichia coli."
    Dubourdieu M., Demoss J.A.
    J. Bacteriol. 174:867-872(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Characterization of NarJ, a system-specific chaperone required for nitrate reductase biogenesis in Escherichia coli."
    Liu X., DeMoss J.A.
    J. Biol. Chem. 272:24266-24271(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CHAPERONE, SUBUNIT, INTERACTION WITH NARG, SUBCELLULAR LOCATION.
  8. "NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli."
    Blasco F., Dos Santos J.P., Magalon A., Frixon C., Guigliarelli B., Santini C.L., Giordano G.
    Mol. Microbiol. 28:435-447(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CHAPERONE, SUBUNIT, INTERACTION WITH NARG.
  9. "Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli."
    Chan C.S., Howell J.M., Workentine M.L., Turner R.J.
    Biochem. Biophys. Res. Commun. 343:244-251(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NARG.
  10. "NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly."
    Vergnes A., Pommier J., Toci R., Blasco F., Giordano G., Magalon A.
    J. Biol. Chem. 281:2170-2176(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH NARG.
    Strain: K12 / MC4100 / JA176.
  11. "Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase."
    Zakian S., Lafitte D., Vergnes A., Pimentel C., Sebban-Kreuzer C., Toci R., Claude J.B., Guerlesquin F., Magalon A.
    FEBS J. 277:1886-1895(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NARG.

Entry informationi

Entry nameiNARJ_ECOLI
AccessioniPrimary (citable) accession number: P0AF26
Secondary accession number(s): P11351
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 20, 2016
This is version 78 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

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.