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Entry version 114 (07 Apr 2021)
Sequence version 1 (06 Dec 2005)
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Protein

Nus factor SuhB

Gene

suhB

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

Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure (PubMed:32871103). Involved in 30S ribosomal subunit biogenesis; thought to be required for loop formation between NusB/NusE (rpsJ, ribosomal protein S10) bound to boxA upstream of the rRNA operons and the elongating RNAP complex. This would promote correct co-transcriptional folding of rRNA. Plays a role in transcription antitermination in a plasmid context in vivo (PubMed:26980831). Required for rrn transcription antitermination; required for integration of NusB/NusE into the antitermination complex (PubMed:31020314). The Nus factor complex (NusA, NusB, NusE (rpsJ), NusG and SuhB) represses expression of suhB and possibly other genes via boxA; the Nus complex prevents or promotes Rho-mediated transcription termination depending on gene context (PubMed:29229908). Involved in post-transcriptional control of gene expression (Probable). Enzymatic activity is not required for complementation of the cold-sensitive phenotype of the dnaB121 mutation (PubMed:10747806) (Probable).6 Publications5 Publications
Has D,L-inositol-1-monophosphatase and beta-glycerophosphatase activity, has less to no activity against a number of other substrates (PubMed:8002619). 2.5-fold more active on 1D-inositol-1-monophosphate than L-inositol-1-monophosphate (1D-myo-inositol 3-phosphate). Specific activity increases significantly upon heating. Only beta-glycerophosphate and adenosine 2'-monophosphate are alternative substrates (PubMed:10747806).2 Publications
Required for growth at low temperatures (PubMed:2138605, PubMed:6389495, PubMed:1847383, PubMed:8002619, PubMed:8589060, PubMed:17652087, PubMed:26980831). Identified as a suppressor (ssyA3) of a temperature-sensitive, protein export missense mutation of secY (secY24), allows growth at 42 but not 30 degrees Celsius (PubMed:6389495). Identified as a suppressor (suhB2) of an rpoH missense mutation (rpoH15), allowing growth at 37 and 40 but not 25, 30 or 34 degrees Celsius, increases expression of RpoH (PubMed:2138605). Identified as a suppressor of a dnaB helicase missense mutation (dnaB121), restores growth at 42 but not 30 degrees Celsius (PubMed:1847383). In both suhB2 and ssyA3 there is an insertion in the 5' region of the gene which prevents SuhB protein expression (PubMed:8002619, PubMed:8589060). Missense mutant suhB10 is suppressed by mutations in RNase III (rnc), showing genetic interaction between them (PubMed:8589060). Deletion of suhB is suppressed by mutations in RNase III, by a mutation in nusA or deletion of nusB, indicating that in the absence of SuhB the Nus complex inhibits growth (PubMed:26980831).7 Publications

Miscellaneous

E.coli makes very low amounts of myo-inositol-containing phospholipids, so the catalytic necessity for this enzyme is low.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+4 PublicationsNote: Partial activity is seen with Co2+, Ni2+, Mn2+, Zn2+ and Fe2+; in the presence of Mg2+ these cations inhibit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by Li+ (PubMed:8002619, PubMed:10747806) (Probable). Li+ binds to Asp-84, Asp-87 and Asp-212 (PubMed:22384802).1 Publication3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=71 µM for myo-inositol phosphate1 Publication
  2. KM=64 µM for 1D-myo-inositol 1-phosphate1 Publication
  3. KM=79 µM for 1D-myo-inositol 3-phosphate1 Publication
  4. KM=69 µM for myo-inositol phosphate1 Publication
  5. KM=92 µM for myo-inositol phosphate after 5 minutes at 70 degrees Celsius1 Publication
  6. KM=110 µM for 1D-myo-inositol 1-phosphate1 Publication
  1. Vmax=12.3 µmol/min/mg enzyme1 Publication
  2. Vmax=6.9 µmol/min/mg enzyme for 1D-myo-inositol 1-phosphate1 Publication
  3. Vmax=2.66 µmol/min/mg enzyme for 1D-myo-inositol 3-phosphate1 Publication
  4. Vmax=3.38 µmol/min/mg enzyme for myo-inositol phosphate1 Publication
  5. Vmax=27.6 µmol/min/mg enzyme for myo-inositol phosphate after 5 minutes at 70 degrees Celsius1 Publication

pH dependencei

Optimum pH is 7.8.1 Publication

Temperature dependencei

Optimum temperature is 80 degrees Celsius, 90% of activity remains after heating at 70 degrees Celsius for 5 minutes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi67Magnesium2 Publications1
<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 sitei67SubstrateBy similarity1
Metal bindingi84Magnesium2 Publications1
Metal bindingi86Magnesium; via carbonyl oxygen2 Publications1
Binding sitei183SubstrateBy similarity1
Binding sitei212SubstrateBy similarity1

<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 functionChaperone, Hydrolase, RNA-binding
Biological processRibosome biogenesis, Transcription, Transcription antitermination, Transcription regulation
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10983-MONOMER
MetaCyc:EG10983-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.3.25, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0ADG4

<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:
Nus factor SuhB1 Publication
Alternative name(s):
Inositol-1-monophosphatase1 Publication (EC:3.1.3.251 Publication)
Short name:
I-1-Pase1 Publication
Short name:
IMPase
Short name:
Inositol-1-phosphatase
<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:suhB1 Publication
Synonyms:ssyA1 Publication
Ordered Locus Names:b2533, JW2517
<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

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

<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

Conditionally lethal, cells are unable to grow at 30 degrees Celsius and less, grow poorly at 37 degrees Celsius, but do grow at 42 degrees Celsius.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi87D → N: Loss of IMPase activity, still complements dnaB121 helicase mutation. 1 Publication1
Mutagenesisi139R → C in suhB10; decreases polypeptide chain elongation rate, grows at 30 but not 25 degrees Celsius; when associated with A-250. 1 Publication1
Mutagenesisi173G → V: No growth at 30 degrees Celsius, IMPase activity not inhibited by RNA polymerase (RNAP). 1 Publication1
Mutagenesisi183R → A: Some growth at 30 degrees Celsius, greater IMPase activity, partially inhibited by RNAP. 1 Publication1
Mutagenesisi184R → A: Grows at 30 degrees Celsius, makes more dimer, partially inhibited by RNAP, crystallizes. 1 Publication1
Mutagenesisi184R → I: No growth at 30 degrees Celsius, IMPase activity not inhibited by RNAP. 1 Publication1
Mutagenesisi250V → A in suhB10; decreases polypeptide chain elongation rate, grows at 30 but not 25 degrees Celsius; when associated with C-139. 1 Publication1
Mutagenesisi251 – 254KAML → AAMA: 3-fold decreased affinity for NusA, less efficient in delaying or suppressing Rho-dependent transcription termination. 1 Publication4

<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_00001425591 – 267Nus factor SuhBAdd BLAST267

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0ADG4

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

More...
PaxDbi
P0ADG4

PRoteomics IDEntifications database

More...
PRIDEi
P0ADG4

2D gel databases

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

More...
SWISS-2DPAGEi
P0ADG4

<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

Transcription is autoregulated (PubMed:8831954). Repressed by the Nus factor complex (NusA, NusB, NusE (rpsJ), NusG and SuhB) (PubMed:29229908).2 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%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

Monomer (PubMed:10747806, PubMed:31127279). A monomer-dimer equilibrium (PubMed:17652087). Homodimer (PubMed:31020314, PubMed:32871103). The rRNA transcription and antitermination complex (rrnTAC) consists of RNA polymerase (RNAP), NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than other subunits (PubMed:31127279, PubMed:31020314, PubMed:32871103). Binds to RNAP, which decreases IMPase activity against 1D-myo-inositol 1-phosphate (PubMed:17652087) (Probable). Association with rRNA gene-transcribing RNAP is dependent on NusB (PubMed:26980831, PubMed:29229908).

Interacts with AR2 domain of NusA; crystallizes as a 2:1 SuhB:NusA heterotrimer (PubMed:31020314, PubMed:31127279).

1 Publication7 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260600, 8 interactors
851613, 5 interactors

Protein interaction database and analysis system

More...
IntActi
P0ADG4, 10 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2533

<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

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P0ADG4

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0ADG4

<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>Regioni86 – 89Substrate bindingBy similarity4

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
COG0483, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_044118_0_4_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0ADG4

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0ADG4

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01639, IMPase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR033942, IMPase
IPR020583, Inositol_monoP_metal-BS
IPR000760, Inositol_monophosphatase-like
IPR020550, Inositol_monophosphatase_CS
IPR022337, Inositol_monophosphatase_SuhB

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00459, Inositol_P, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00377, IMPHPHTASES
PR01959, SBIMPHPHTASE

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00629, IMP_1, 1 hit
PS00630, IMP_2, 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.

P0ADG4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHPMLNIAVR AARKAGNLIA KNYETPDAVE ASQKGSNDFV TNVDKAAEAV
60 70 80 90 100
IIDTIRKSYP QHTIITEESG ELEGTDQDVQ WVIDPLDGTT NFIKRLPHFA
110 120 130 140 150
VSIAVRIKGR TEVAVVYDPM RNELFTATRG QGAQLNGYRL RGSTARDLDG
160 170 180 190 200
TILATGFPFK AKQYATTYIN IVGKLFNECA DFRRTGSAAL DLAYVAAGRV
210 220 230 240 250
DGFFEIGLRP WDFAAGELLV REAGGIVSDF TGGHNYMLTG NIVAGNPRVV
260
KAMLANMRDE LSDALKR
Length:267
Mass (Da):29,172
Last modified:December 6, 2005 - 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:i8FEC3508BD111301
GO

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 conflicti141R → L in AAA67506 (PubMed:2138605).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M34828 Genomic DNA Translation: AAA67506.1
U00096 Genomic DNA Translation: AAC75586.1
AP009048 Genomic DNA Translation: BAA16427.1

Protein sequence database of the Protein Information Resource

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PIRi
D65030

NCBI Reference Sequences

More...
RefSeqi
NP_417028.1, NC_000913.3
WP_000553451.1, NZ_STEB01000011.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75586; AAC75586; b2533
BAA16427; BAA16427; BAA16427

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
58460715
947285

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2517
eco:b2533

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4201

<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
M34828 Genomic DNA Translation: AAA67506.1
U00096 Genomic DNA Translation: AAC75586.1
AP009048 Genomic DNA Translation: BAA16427.1
PIRiD65030
RefSeqiNP_417028.1, NC_000913.3
WP_000553451.1, NZ_STEB01000011.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QFLX-ray1.90A1-267[»]
6IB7X-ray2.25A1-267[»]
6IB8X-ray1.65A/B1-267[»]
6TQNelectron microscopy3.80S/T1-267[»]
6TQOelectron microscopy4.00S/T1-267[»]
SMRiP0ADG4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260600, 8 interactors
851613, 5 interactors
IntActiP0ADG4, 10 interactors
STRINGi511145.b2533

2D gel databases

SWISS-2DPAGEiP0ADG4

Proteomic databases

jPOSTiP0ADG4
PaxDbiP0ADG4
PRIDEiP0ADG4

Genome annotation databases

EnsemblBacteriaiAAC75586; AAC75586; b2533
BAA16427; BAA16427; BAA16427
GeneIDi58460715
947285
KEGGiecj:JW2517
eco:b2533
PATRICifig|1411691.4.peg.4201

Organism-specific databases

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

More...
EchoBASEi
EB0976

Phylogenomic databases

eggNOGiCOG0483, Bacteria
HOGENOMiCLU_044118_0_4_6
InParanoidiP0ADG4
PhylomeDBiP0ADG4

Enzyme and pathway databases

BioCyciEcoCyc:EG10983-MONOMER
MetaCyc:EG10983-MONOMER
BRENDAi3.1.3.25, 2026
SABIO-RKiP0ADG4

Miscellaneous databases

EvolutionaryTraceiP0ADG4

Protein Ontology

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PROi
PR:P0ADG4

Family and domain databases

CDDicd01639, IMPase, 1 hit
InterProiView protein in InterPro
IPR033942, IMPase
IPR020583, Inositol_monoP_metal-BS
IPR000760, Inositol_monophosphatase-like
IPR020550, Inositol_monophosphatase_CS
IPR022337, Inositol_monophosphatase_SuhB
PfamiView protein in Pfam
PF00459, Inositol_P, 1 hit
PRINTSiPR00377, IMPHPHTASES
PR01959, SBIMPHPHTASE
PROSITEiView protein in PROSITE
PS00629, IMP_1, 1 hit
PS00630, IMP_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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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 nameiSUHB_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: P0ADG4
Secondary accession number(s): P22783, P77511, Q8X2E6
<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: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 7, 2021
This is version 114 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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