NARJ_ECOLI
ID NARJ_ECOLI Reviewed; 236 AA.
AC P0AF26; P11351;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Nitrate reductase molybdenum cofactor assembly chaperone NarJ;
DE AltName: Full=Redox enzyme maturation protein NarJ;
GN Name=narJ; OrderedLocusNames=b1226, JW1217;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2832376; DOI=10.1128/jb.170.4.1721-1729.1988;
RA Sodergren E.J., Demoss J.A.;
RT "narI region of the Escherichia coli nitrate reductase (nar) operon
RT contains two genes.";
RL J. Bacteriol. 170:1721-1729(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RC STRAIN=K12 / TG1;
RX PubMed=2674654; DOI=10.1007/bf00331275;
RA Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.;
RT "Nitrate reductase of Escherichia coli: completion of the nucleotide
RT sequence of the nar operon and reassessment of the role of the alpha and
RT beta subunits in iron binding and electron transfer.";
RL Mol. Gen. Genet. 218:249-256(1989).
RN [6]
RP FUNCTION.
RX PubMed=1732220; DOI=10.1128/jb.174.3.867-872.1992;
RA Dubourdieu M., Demoss J.A.;
RT "The narJ gene product is required for biogenesis of respiratory nitrate
RT reductase in Escherichia coli.";
RL J. Bacteriol. 174:867-872(1992).
RN [7]
RP FUNCTION AS A CHAPERONE, SUBUNIT, INTERACTION WITH NARG, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9305880; DOI=10.1074/jbc.272.39.24266;
RA Liu X., DeMoss J.A.;
RT "Characterization of NarJ, a system-specific chaperone required for nitrate
RT reductase biogenesis in Escherichia coli.";
RL J. Biol. Chem. 272:24266-24271(1997).
RN [8]
RP FUNCTION AS A CHAPERONE, SUBUNIT, AND INTERACTION WITH NARG.
RX PubMed=9632249; DOI=10.1046/j.1365-2958.1998.00795.x;
RA Blasco F., Dos Santos J.P., Magalon A., Frixon C., Guigliarelli B.,
RA Santini C.L., Giordano G.;
RT "NarJ is a specific chaperone required for molybdenum cofactor assembly in
RT nitrate reductase A of Escherichia coli.";
RL Mol. Microbiol. 28:435-447(1998).
RN [9]
RP INTERACTION WITH NARG.
RX PubMed=16540088; DOI=10.1016/j.bbrc.2006.02.133;
RA Chan C.S., Howell J.M., Workentine M.L., Turner R.J.;
RT "Twin-arginine translocase may have a role in the chaperone function of
RT NarJ from Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 343:244-251(2006).
RN [10]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH NARG.
RC STRAIN=K12 / MC4100 / JA176;
RX PubMed=16286471; DOI=10.1074/jbc.m505902200;
RA Vergnes A., Pommier J., Toci R., Blasco F., Giordano G., Magalon A.;
RT "NarJ chaperone binds on two distinct sites of the aponitrate reductase of
RT Escherichia coli to coordinate molybdenum cofactor insertion and
RT assembly.";
RL J. Biol. Chem. 281:2170-2176(2006).
RN [11]
RP INTERACTION WITH NARG.
RX PubMed=20236317; DOI=10.1111/j.1742-4658.2010.07611.x;
RA Zakian S., Lafitte D., Vergnes A., Pimentel C., Sebban-Kreuzer C., Toci R.,
RA Claude J.B., Guerlesquin F., Magalon A.;
RT "Basis of recognition between the NarJ chaperone and the N-terminus of the
RT NarG subunit from Escherichia coli nitrate reductase.";
RL FEBS J. 277:1886-1895(2010).
CC -!- FUNCTION: Chaperone required for proper molybdenum cofactor insertion
CC and final assembly of the membrane-bound respiratory nitrate reductase
CC 1. Required for the insertion of the molybdenum into the apo-NarG
CC subunit, maybe by keeping NarG in an appropriate competent-open
CC conformation for the molybdenum cofactor insertion to occur. NarJ
CC maintains the apoNarGH complex in a soluble state. Upon insertion of
CC the molybdenum cofactor, NarJ seems to dissociate from the activated
CC soluble NarGH complex, before its association with the NarI subunit on
CC the membrane. {ECO:0000269|PubMed:16286471, ECO:0000269|PubMed:1732220,
CC ECO:0000269|PubMed:9305880, ECO:0000269|PubMed:9632249}.
CC -!- SUBUNIT: Binds specifically to the NarG subunit of the apoenzyme
CC complex at two distinct sites, one interfering with membrane anchoring
CC and another being involved in molybdenum insertion.
CC {ECO:0000269|PubMed:16286471, ECO:0000269|PubMed:9305880,
CC ECO:0000269|PubMed:9632249}.
CC -!- INTERACTION:
CC P0AF26; P09152: narG; NbExp=18; IntAct=EBI-555043, EBI-547248;
CC P0AF26; P19319: narZ; NbExp=3; IntAct=EBI-555043, EBI-547262;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9305880}.
CC -!- SIMILARITY: Belongs to the NarJ/NarW family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M20147; AAA24196.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74310.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36096.1; -; Genomic_DNA.
DR EMBL; X16181; CAA34305.1; -; Genomic_DNA.
DR PIR; B27737; BVECJ.
DR RefSeq; NP_415744.1; NC_000913.3.
DR RefSeq; WP_000571681.1; NZ_SSZK01000010.1.
DR AlphaFoldDB; P0AF26; -.
DR SMR; P0AF26; -.
DR BioGRID; 4262232; 15.
DR BioGRID; 850174; 1.
DR DIP; DIP-35943N; -.
DR IntAct; P0AF26; 11.
DR MINT; P0AF26; -.
DR STRING; 511145.b1226; -.
DR jPOST; P0AF26; -.
DR PaxDb; P0AF26; -.
DR PRIDE; P0AF26; -.
DR EnsemblBacteria; AAC74310; AAC74310; b1226.
DR EnsemblBacteria; BAA36096; BAA36096; BAA36096.
DR GeneID; 945807; -.
DR KEGG; ecj:JW1217; -.
DR KEGG; eco:b1226; -.
DR PATRIC; fig|1411691.4.peg.1055; -.
DR EchoBASE; EB0635; -.
DR eggNOG; COG2180; Bacteria.
DR HOGENOM; CLU_084469_0_0_6; -.
DR InParanoid; P0AF26; -.
DR OMA; CELFDRG; -.
DR PhylomeDB; P0AF26; -.
DR BioCyc; EcoCyc:NARJ-MON; -.
DR BRENDA; 1.7.5.1; 2026.
DR PRO; PR:P0AF26; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016530; F:metallochaperone activity; IMP:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:UniProtKB.
DR GO; GO:0042128; P:nitrate assimilation; IDA:UniProtKB.
DR InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR InterPro; IPR003765; NO3_reductase_chaperone_NarJ.
DR InterPro; IPR036411; TorD-like_sf.
DR PANTHER; PTHR43680; PTHR43680; 1.
DR Pfam; PF02613; Nitrate_red_del; 1.
DR SUPFAM; SSF89155; SSF89155; 1.
DR TIGRFAMs; TIGR00684; narJ; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Nitrate assimilation; Reference proteome.
FT CHAIN 1..236
FT /note="Nitrate reductase molybdenum cofactor assembly
FT chaperone NarJ"
FT /id="PRO_0000096725"
SQ SEQUENCE 236 AA; 26449 MW; 17306C34A57DF1E2 CRC64;
MIELVIVSRL LEYPDAALWQ HQQEMFEAIA ASKNLPKEDA HALGIFLRDL TTMDPLDAQA
QYSELFDRGR ATSLLLFEHV HGESRDRGQA MVDLLAQYEQ HGLQLNSREL PDHLPLYLEY
LAQLPQSEAV EGLKDIAPIL ALLSARLQQR ESRYAVLFDL LLKLANTAID SDKVAEKIAD
EARDDTPQAL DAVWEEEQVK FFADKGCGDS AITAHQRRFA GAVAPQYLNI TTGGQH
