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   02-SEP-2026, entry version 126.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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}.
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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_CP009789.1.
DR   PDB; 8JZD; X-ray; 2.45 A; A/C=1-183.
DR   AlphaFoldDB; P0AF26; -.
DR   SMR; P0AF26; -.
DR   BioGRID; 4262232; 16.
DR   BioGRID; 850174; 1.
DR   DIP; DIP-35943N; -.
DR   FunCoup; P0AF26; 220.
DR   IntAct; P0AF26; 11.
DR   MINT; P0AF26; -.
DR   STRING; 511145.b1226; -.
DR   jPOST; P0AF26; -.
DR   PaxDb; 511145-b1226; -.
DR   EnsemblBacteria; AAC74310; AAC74310; b1226.
DR   GeneID; 945807; -.
DR   KEGG; ecj:JW1217; -.
DR   KEGG; eco:b1226; -.
DR   KEGG; ecoc:C3026_07210; -.
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   OrthoDB; 8478585at2; -.
DR   PhylomeDB; P0AF26; -.
DR   BioCyc; EcoCyc:NARJ-MONOMER; -.
DR   BRENDA; 1.7.5.1; 2026.
DR   PHI-base; PHI:10514; -.
DR   PRO; PR:P0AF26; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0AF26; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016530; F:metallochaperone activity; IMP:EcoCyc.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:UniProtKB.
DR   GO; GO:0042128; P:nitrate assimilation; IDA:UniProtKB.
DR   FunFam; 1.10.3480.10:FF:000001; Nitrate reductase molybdenum cofactor assembly chaperone; 1.
DR   Gene3D; 1.10.3480.10; TorD-like; 1.
DR   InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR   InterPro; IPR003765; NO3_reductase_chaperone_NarJ.
DR   InterPro; IPR036411; TorD-like_sf.
DR   NCBIfam; TIGR00684; narJ; 1.
DR   PANTHER; PTHR43680; NITRATE REDUCTASE MOLYBDENUM COFACTOR ASSEMBLY CHAPERONE; 1.
DR   PANTHER; PTHR43680:SF2; NITRATE REDUCTASE MOLYBDENUM COFACTOR ASSEMBLY CHAPERONE NARJ; 1.
DR   Pfam; PF02613; Nitrate_red_del; 1.
DR   SUPFAM; SSF89155; TorD-like; 1.
DR   PDBsum; 8JZD; -.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Nitrate assimilation;
KW   Reference proteome.
FT   CHAIN           1..236
FT                   /note="Nitrate reductase molybdenum cofactor assembly
FT                   chaperone NarJ"
FT                   /id="PRO_0000096725"
FT   HELIX           2..11
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           16..20
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           22..30
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           37..52
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           55..66
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           84..100
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           126..149
FT                   /evidence="ECO:0007829|PDB:8JZD"
FT   HELIX           155..165
FT                   /evidence="ECO:0007829|PDB:8JZD"
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
//