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Entry version 60 (07 Apr 2021)
Sequence version 1 (15 Jun 2010)
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Protein

Truncated inactive ribonuclease PH

Gene

rph

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

This an expressed but non-active exoribonuclease allele (PubMed:8501045). The catalytically inactive protein translated in strain K12 MG1655 inhibits the 5'-processing of primary pre-tRNAs with short (<5 nucleotide) leaders in a dominant-negative effect when RNA pyrophosphohydrolase (rppH) is also inactive; perhaps inactive Rph inhibits interaction with RNase P which is exacerbated when RppH cannot cleave the triphosphate of the primary transcript (PubMed:28808133).2 Publications

Miscellaneous

The gene in K12 strains MG1655 and W3110 (and also other derivatives of K12 W1485) has a frameshift mutation that leads to loss of activity, although the protein is translated. Thus in those strains rph is an expressed, catalytically inactive protein (PubMed:8501045). In strain K12 / MG1655(Seq)* the wild-type protein has been restored (PubMed:21135037, PubMed:27298395, PubMed:28625967). For the functional protein without the frameshift mutation see AC P0CG18.4 Publications
The (restored) wild-type protein plays a significant role in tRNA 3'-end maturation when a C nucleotide follows the mature CCA terminus (PubMed:28808133). Wild-type (restored) protein also plays a critical role in initiating 16S rRNA degradation (leading to ribosome degradation) during starvation, but not in rRNA quality control during steady state growth (PubMed:21135037, PubMed:27298395). The wild-type (restored) protein is rapidly turned over at 42 degrees Celsius during starvation, but not at 31 degrees Celsius with or without starvation; in the absence of RNase 2 (rnb) protein levels do not decline (at protein level) (PubMed:28625967).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei86Phosphate (substrate) bindingUniRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding, tRNA-binding
Biological processrRNA processing, tRNA processing

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10863-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Truncated inactive ribonuclease PH
Short name:
Truncated inactive RNase PH
Alternative name(s):
Inactive RNase PH1 Publication
Truncated RNase PH1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:rph1 PublicationUniRule annotation
Synonyms:orfE
Ordered Locus Names:b3643, JW3618
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

When the gene is deleted the strain no longer inhibits 5'-processing of pre-tRNAs with short (<5 nucleotide) leaders in the absence of rppH (PubMed:28808133). The truncated allele encoded by this protein has a slight growth defect, which is slightly exacerbated when combined with an rppH deletion (PubMed:28808133). The truncated allele suppresses the loss of viability conferred by deletion of RNase 2 (rnb) during stationary phase at 31 and 42 degrees Celsius or starvation at 42 degrees Celsius (PubMed:28625967).2 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001398891 – 228Truncated inactive ribonuclease PHAdd BLAST228

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0CG19

PRoteomics IDEntifications database

More...
PRIDEi
P0CG19

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

The catalytically inactive protein is present at significantly lower levels than restored wild-type protein (at protein level) (PubMed:28808133).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity). No interaction between the inactive protein and RppH or RNase P was detected by immunoprecipitation (PubMed:28808133).

UniRule annotation1 Publication

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-10738N

Protein interaction database and analysis system

More...
IntActi
P0CG19, 9 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0CG19

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni124 – 126Phosphate (substrate) bindingUniRule annotation3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RNase PH family.UniRule annotation

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0CG19

Family and domain databases

Conserved Domains Database

More...
CDDi
cd11362, RNase_PH_bact, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.70, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00564, RNase_PH, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001247, ExoRNase_PH_dom1
IPR015847, ExoRNase_PH_dom2
IPR036345, ExoRNase_PH_dom2_sf
IPR027408, PNPase/RNase_PH_dom_sf
IPR020568, Ribosomal_S5_D2-typ_fold
IPR002381, RNase_PH_bac-type
IPR018336, RNase_PH_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01138, RNase_PH, 1 hit
PF03725, RNase_PH_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211, SSF54211, 1 hit
SSF55666, SSF55666, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01966, RNasePH, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01277, RIBONUCLEASE_PH, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0CG19-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRPAGRSNNQ VRPVTLTRNY TKHAEGSVLV EFGDTKVLCT ASIEEGVPRF
60 70 80 90 100
LKGQGQGWIT AEYGMLPRST HTRNAREAAK GKQGGRTMEI QRLIARALRA
110 120 130 140 150
AVDLKALGEF TITLDCDVLQ ADGGTRTASI TGACVALVDA LQKLVENGKL
160 170 180 190 200
KTNPMKGMVA AVSVGIVNGE AVCDLEYVED SAAETDMNVV MTEDGRIIEV
210 220
QGTAEGEPFT HEELLILLAL ARGESNPL
Length:228
Mass (Da):24,425
Last modified:June 15, 2010 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i028BC8F5A6859447
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
V01578 Genomic DNA No translation available.
L10328 Genomic DNA Translation: AAA61996.1
U00096 Genomic DNA Translation: AYC08250.1
AP009048 Genomic DNA No translation available.
X72920 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
A04470, QQECPE

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AYC08250; AYC08250; b3643

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01578 Genomic DNA No translation available.
L10328 Genomic DNA Translation: AAA61996.1
U00096 Genomic DNA Translation: AYC08250.1
AP009048 Genomic DNA No translation available.
X72920 Genomic DNA No translation available.
PIRiA04470, QQECPE

3D structure databases

SMRiP0CG19
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-10738N
IntActiP0CG19, 9 interactors

Proteomic databases

PaxDbiP0CG19
PRIDEiP0CG19

Genome annotation databases

EnsemblBacteriaiAYC08250; AYC08250; b3643

Phylogenomic databases

InParanoidiP0CG19

Enzyme and pathway databases

BioCyciEcoCyc:EG10863-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0CG19

Family and domain databases

CDDicd11362, RNase_PH_bact, 1 hit
Gene3Di3.30.230.70, 1 hit
HAMAPiMF_00564, RNase_PH, 1 hit
InterProiView protein in InterPro
IPR001247, ExoRNase_PH_dom1
IPR015847, ExoRNase_PH_dom2
IPR036345, ExoRNase_PH_dom2_sf
IPR027408, PNPase/RNase_PH_dom_sf
IPR020568, Ribosomal_S5_D2-typ_fold
IPR002381, RNase_PH_bac-type
IPR018336, RNase_PH_CS
PfamiView protein in Pfam
PF01138, RNase_PH, 1 hit
PF03725, RNase_PH_C, 1 hit
SUPFAMiSSF54211, SSF54211, 1 hit
SSF55666, SSF55666, 1 hit
TIGRFAMsiTIGR01966, RNasePH, 1 hit
PROSITEiView protein in PROSITE
PS01277, RIBONUCLEASE_PH, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRNPH_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0CG19
Secondary accession number(s): A0A385XJN7, A8DYQ0, P03842
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: April 7, 2021
This is version 60 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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