rnpA

rnpA
168

protein component of RNase P, metal-dependent 5 end maturation of precursor tRNAs

locus
BSU_41050
Molecular weight
13.66 kDa
pI
10.8
Protein length
Gene length
function
cleavage of precursor sequences from the 5 ends of pre-tRNAs
product
protein component of RNase P (substrate specificity)
essential
yes
ec
3.1.26.5
synonyms
rnpA

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0594 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
4,214,753  4,215,103
Phenotypes of a mutant
essential [Pubmed|12682299]
The protein
Catalyzed reaction/ biological activity
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor (according to UniProt)
5' end maturation of tmRNA [Pubmed|25402410]
Protein family
RnpA family (single member, according to UniProt)
[wiki|Domains]
RNR motif: residues 60-68, stabilizes complexes with both RNA part of [wiki|RNase] P (''[gene|57A79AAF00243B5E058FA901D43AA7B55CA33F63|rnpB]'') and with pre-[gene|3B6620F44EC08BA9B02FE9359A5F74C6CAE6D4FB|trnA-Ile] ([gene|57A79AAF00243B5E058FA901D43AA7B55CA33F63|rnpB]-[protein|594F2D36BE71A45303A33AA2A2931F56F0A969ED|rnpA]-pre-[gene|3B6620F44EC08BA9B02FE9359A5F74C6CAE6D4FB|trnA-Ile]) [Pubmed|21622899]
Structure
[PDB|1A6F]  [Pubmed|9563955]
[PDB|3Q1R] (complex of RnpA with RNA [protein|57A79AAF00243B5E058FA901D43AA7B55CA33F63|rnpB] and [gene|3B6620F44EC08BA9B02FE9359A5F74C6CAE6D4FB|trnA-Ile], from ''Thermotoga maritima'') [Pubmed|21076397]
[AF|P25814]
Kinetic information
KD ([protein|594F2D36BE71A45303A33AA2A2931F56F0A969ED|rnpA]-[protein|57A79AAF00243B5E058FA901D43AA7B55CA33F63|rnpB] interaction): 40 nM [pubmed|15337847]
Expression and Regulation
Operons
genes
[gene|EB07AECD3849CC0B65126DE27E71B28B3AD106B0|rpmH]-[gene|594F2D36BE71A45303A33AA2A2931F56F0A969ED|rnpA]-[gene|D40C202E67A5319A91811DB11356F47A56C97DD2|yidC1]-[gene|23D33E2D7AB1CA02165070DB8238957E3C768E64|jag]
description
[Pubmed|22383849]
regulation
expression is reduced in motile cells as compared to non-motile cells [pubmed|33782055]
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[gene|EB07AECD3849CC0B65126DE27E71B28B3AD106B0|rpmH]→[gene|23D33E2D7AB1CA02165070DB8238957E3C768E64|jag]

2024-10-05 03:47:45

Jstuelk

119

E083541B5FC7B773C237692E19D8D077A360C15A

091CC69B9E971C4FEAD3C4AEC4A1CDFAE7D6AF75

Biological materials
two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system ([wiki|BACTH]), available in [wiki|Jörg Stülke]'s lab
labs
[wiki|Carol Fierke], University of Michigan, Ann Arbor, USA [https://www.chem.lsa.umich.edu/chem/faculty/facultyDetail.php?Uniqname=fierke homepage]
[wiki|Roland Hartmann], Marburg University, Germany [http://www.pharmazie.uni-marburg.de/pharmchem/akhartmann/ag_hartmann.htm homepage]
References
Reviews
19215776,8901495,17868095,14691942,16650980,16980936,16679018,14550630,31464530,35787606,38479802
Original Publications
10390342,17919279,17355991,11812129,16980484,11454206,19549719,11454206,9563955,19932118,17299131,20476778,11258888,16185070,21764917,22848659,21076397,20843005,21622899,24364358,25249623,25402410,26267651,27873254,31003868,31993626,33972249,12390025,11233980,15337847

594F2D36BE71A45303A33AA2A2931F56F0A969ED

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Time of last update: 2024-10-05 12:06:07

Author of last update: Jstuelk