Tag | Content |
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CPLM ID | CPLM-003516 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Nitrate reductase molybdenum cofactor assembly chaperone NarJ |
Protein Synonyms/Alias | Redox enzyme maturation protein NarJ |
Gene Name | narJ |
Gene Synonyms/Alias | b1226; JW1217 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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37 | AASKNLPKEDAHALG | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | 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. |
Sequence Annotation | |
Keyword | Chaperone; Complete proteome; Cytoplasm; Nitrate assimilation; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 236 AA |
Protein Sequence | MIELVIVSRL LEYPDAALWQ HQQEMFEAIA ASKNLPKEDA HALGIFLRDL TTMDPLDAQA 60 QYSELFDRGR ATSLLLFEHV HGESRDRGQA MVDLLAQYEQ HGLQLNSREL PDHLPLYLEY 120 LAQLPQSEAV EGLKDIAPIL ALLSARLQQR ESRYAVLFDL LLKLANTAID SDKVAEKIAD 180 EARDDTPQAL DAVWEEEQVK FFADKGCGDS AITAHQRRFA GAVAPQYLNI TTGGQH 236 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:UniProtKB. GO:0016530; F:metallochaperone activity; IMP:EcoCyc. GO:0051131; P:chaperone-mediated protein complex assembly; IDA:UniProtKB. GO:0042128; P:nitrate assimilation; IDA:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |