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Protein

Polyribonucleotide nucleotidyltransferase

Gene

pnp

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

Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. Also involved, along with RNase II, in tRNA processing. RNases II and R contribute to rRNA degradation during starvation, while RNase R and PNPase are the major contributors to quality control of rRNA during steady state growth (PubMed:21135037).UniRule annotation6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotation1 Publication, Mn2+UniRule annotation1 PublicationNote: Magnesium. Can also use manganese.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi486Magnesium1 Publication1
Metal bindingi492Magnesium1 Publication1

<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

  • mRNA catabolic process Source: UniProtKB-UniRule
  • response to heat Source: EcoCyc
  • RNA catabolic process Source: GO_Central
  • RNA processing Source: InterPro

<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 functionNucleotidyltransferase, RNA-binding, Transferase
Biological processStress response
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10743-MONOMER
MetaCyc:EG10743-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.8 2026

<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_and_taxonomy_section">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:
Polyribonucleotide nucleotidyltransferaseUniRule annotation (EC:2.7.7.8UniRule annotation3 Publications)
Alternative name(s):
Polynucleotide phosphorylaseUniRule annotation
Short name:
PNPaseUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:pnpUniRule annotation
Ordered Locus Names:b3164, JW5851
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10743 pnp

<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

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi79 – 80RR → AA: Strongly reduces RNA binding. Reduces RNA degradation. 1 Publication2
Mutagenesisi83R → A: No effect on RNA-binding. No effect on degradation of long RNA molecules. Impairs degradation of short RNA molecules. 1 Publication1
Mutagenesisi100R → D: Abolishes enzyme activity. 1 Publication1
Mutagenesisi319R → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi398 – 399RR → DD: Abolishes enzyme activity. 2
Mutagenesisi428V → P: Abolishes enzyme activity. 1 Publication1
Mutagenesisi444C → W: Abolishes enzyme activity. 1 Publication1
Mutagenesisi492D → G: Abolishes enzyme activity. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001979131 – 711Polyribonucleotide nucleotidyltransferaseAdd BLAST711

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P05055

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

More...
PaxDbi
P05055

PRoteomics IDEntifications database

More...
PRIDEi
P05055

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P05055

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P05055

<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

Expression is negatively autoregulated at the translational level via an RNase III-dependent mechanism. Induced by cold shock (42 to 15 degrees Celsius) (at protein level) (PubMed:8898389). At low temperature, the destabilizing effect of PNPase on its own mRNA is less efficient, leading to a decrease in repression and an increase in the expression level.3 Publications

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Interacts with RNase E (rne). Homotrimer. The homotrimer forms a ring-like structure with a central channel, where RNA molecules can bind. RNA molecules bind between neighboring subunits.UniRule annotation6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262431, 94 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-403 Degradosome

Database of interacting proteins

More...
DIPi
DIP-10522N

Protein interaction database and analysis system

More...
IntActi
P05055, 45 interactors

Molecular INTeraction database

More...
MINTi
P05055

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_3337

<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

Secondary structure

1711
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P05055

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

More...
SMRi
P05055

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P05055

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini553 – 612KHUniRule annotationAdd BLAST60
Domaini622 – 690S1 motifUniRule annotationAdd BLAST69

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>Regioni77 – 80FFRR loop; important for RNA binding1 Publication4
Regioni327 – 331Interaction with RNase E1 Publication5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The S1 motif domain is important for trimerization and RNA-binding.1 Publication

<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 polyribonucleotide nucleotidyltransferase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C62 Bacteria
COG1185 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000218327

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P05055

KEGG Orthology (KO)

More...
KOi
K00962

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P05055

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1370.10, 1 hit
3.30.230.70, 2 hits

HAMAP database of protein families

More...
HAMAPi
MF_01595 PNPase, 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
IPR004087 KH_dom
IPR004088 KH_dom_type_1
IPR036612 KH_dom_type_1_sf
IPR012340 NA-bd_OB-fold
IPR012162 PNPase
IPR027408 PNPase/RNase_PH_dom_sf
IPR015848 PNPase_PH_RNA-bd_bac/org-type
IPR036456 PNPase_PH_RNA-bd_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR022967 S1_dom
IPR003029 S1_domain

The PANTHER Classification System

More...
PANTHERi
PTHR11252 PTHR11252, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00013 KH_1, 1 hit
PF03726 PNPase, 1 hit
PF01138 RNase_PH, 2 hits
PF03725 RNase_PH_C, 2 hits
PF00575 S1, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005499 PNPase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00322 KH, 1 hit
SM00316 S1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46915 SSF46915, 1 hit
SSF50249 SSF50249, 1 hit
SSF54211 SSF54211, 2 hits
SSF54791 SSF54791, 1 hit
SSF55666 SSF55666, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03591 polynuc_phos, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50084 KH_TYPE_1, 1 hit
PS50126 S1, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P05055-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGQKKA
60 70 80 90 100
KPGQDFFPLT VNYQERTYAA GRIPGSFFRR EGRPSEGETL IARLIDRPIR
110 120 130 140 150
PLFPEGFVNE VQVIATVVSV NPQVNPDIVA MIGASAALSL SGIPFNGPIG
160 170 180 190 200
AARVGYINDQ YVLNPTQDEL KESKLDLVVA GTEAAVLMVE SEAQLLSEDQ
210 220 230 240 250
MLGAVVFGHE QQQVVIQNIN ELVKEAGKPR WDWQPEPVNE ALNARVAALA
260 270 280 290 300
EARLSDAYRI TDKQERYAQV DVIKSETIAT LLAEDETLDE NELGEILHAI
310 320 330 340 350
EKNVVRSRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA
360 370 380 390 400
LVTATLGTAR DAQVLDELMG ERTDTFLFHY NFPPYSVGET GMVGSPKRRE
410 420 430 440 450
IGHGRLAKRG VLAVMPDMDK FPYTVRVVSE ITESNGSSSM ASVCGASLAL
460 470 480 490 500
MDAGVPIKAA VAGIAMGLVK EGDNYVVLSD ILGDEDHLGD MDFKVAGSRD
510 520 530 540 550
GISALQMDIK IEGITKEIMQ VALNQAKGAR LHILGVMEQA INAPRGDISE
560 570 580 590 600
FAPRIHTIKI NPDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT
610 620 630 640 650
DGEKAKHAIR RIEEITAEIE VGRVYTGKVT RIVDFGAFVA IGGGKEGLVH
660 670 680 690 700
ISQIADKRVE KVTDYLQMGQ EVPVKVLEVD RQGRIRLSIK EATEQSQPAA
710
APEAPAAEQG E
Length:711
Mass (Da):77,101
Last modified:November 1, 1995 - v3
<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:i785B7D54716FC2DE
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA57967 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE77210 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti357G → R in AAA83905 (PubMed:2432069).Curated1
Sequence conflicti450L → S in AAA83905 (PubMed:2432069).Curated1

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
J02638 Genomic DNA Translation: AAA83905.1
U18997 Genomic DNA Translation: AAA57967.1 Different initiation.
U00096 Genomic DNA Translation: AAC76198.2
AP009048 Genomic DNA Translation: BAE77210.1 Different initiation.
X00761 Genomic DNA Translation: CAA25332.1
M14425 Genomic DNA Translation: AAA24596.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H65106

NCBI Reference Sequences

More...
RefSeqi
NP_417633.4, NC_000913.3
WP_001295554.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76198; AAC76198; b3164
BAE77210; BAE77210; BAE77210

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947672

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5851
eco:b3164

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3566

<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
J02638 Genomic DNA Translation: AAA83905.1
U18997 Genomic DNA Translation: AAA57967.1 Different initiation.
U00096 Genomic DNA Translation: AAC76198.2
AP009048 Genomic DNA Translation: BAE77210.1 Different initiation.
X00761 Genomic DNA Translation: CAA25332.1
M14425 Genomic DNA Translation: AAA24596.1
PIRiH65106
RefSeqiNP_417633.4, NC_000913.3
WP_001295554.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SRONMR-A617-692[»]
3CDIX-ray2.60A2-711[»]
3CDJX-ray2.80A2-547[»]
3GCMX-ray2.50A/B/C1-549[»]
3GLLX-ray2.70A1-549[»]
3GMEX-ray2.40A1-549[»]
3H1CX-ray3.57A/B/C/G/I/K/M/O/R/T/V/X1-549[»]
ProteinModelPortaliP05055
SMRiP05055
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262431, 94 interactors
ComplexPortaliCPX-403 Degradosome
DIPiDIP-10522N
IntActiP05055, 45 interactors
MINTiP05055
STRINGi316385.ECDH10B_3337

PTM databases

CarbonylDBiP05055

2D gel databases

SWISS-2DPAGEiP05055

Proteomic databases

EPDiP05055
PaxDbiP05055
PRIDEiP05055

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76198; AAC76198; b3164
BAE77210; BAE77210; BAE77210
GeneIDi947672
KEGGiecj:JW5851
eco:b3164
PATRICifig|1411691.4.peg.3566

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0736
EcoGeneiEG10743 pnp

Phylogenomic databases

eggNOGiENOG4105C62 Bacteria
COG1185 LUCA
HOGENOMiHOG000218327
InParanoidiP05055
KOiK00962
PhylomeDBiP05055

Enzyme and pathway databases

BioCyciEcoCyc:EG10743-MONOMER
MetaCyc:EG10743-MONOMER
BRENDAi2.7.7.8 2026

Miscellaneous databases

EvolutionaryTraceiP05055

Protein Ontology

More...
PROi
PR:P05055

Family and domain databases

Gene3Di3.30.1370.10, 1 hit
3.30.230.70, 2 hits
HAMAPiMF_01595 PNPase, 1 hit
InterProiView protein in InterPro
IPR001247 ExoRNase_PH_dom1
IPR015847 ExoRNase_PH_dom2
IPR036345 ExoRNase_PH_dom2_sf
IPR004087 KH_dom
IPR004088 KH_dom_type_1
IPR036612 KH_dom_type_1_sf
IPR012340 NA-bd_OB-fold
IPR012162 PNPase
IPR027408 PNPase/RNase_PH_dom_sf
IPR015848 PNPase_PH_RNA-bd_bac/org-type
IPR036456 PNPase_PH_RNA-bd_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR022967 S1_dom
IPR003029 S1_domain
PANTHERiPTHR11252 PTHR11252, 1 hit
PfamiView protein in Pfam
PF00013 KH_1, 1 hit
PF03726 PNPase, 1 hit
PF01138 RNase_PH, 2 hits
PF03725 RNase_PH_C, 2 hits
PF00575 S1, 1 hit
PIRSFiPIRSF005499 PNPase, 1 hit
SMARTiView protein in SMART
SM00322 KH, 1 hit
SM00316 S1, 1 hit
SUPFAMiSSF46915 SSF46915, 1 hit
SSF50249 SSF50249, 1 hit
SSF54211 SSF54211, 2 hits
SSF54791 SSF54791, 1 hit
SSF55666 SSF55666, 2 hits
TIGRFAMsiTIGR03591 polynuc_phos, 1 hit
PROSITEiView protein in PROSITE
PS50084 KH_TYPE_1, 1 hit
PS50126 S1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<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 nameiPNP_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: P05055
Secondary accession number(s): P78109, Q2M946
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1995
Last modified: December 5, 2018
This is version 188 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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