UniProtKB - P0ADG4 (SUHB_ECOLI)
Nus factor SuhB
suhB
Functioni
Miscellaneous
Catalytic activityi
Cofactori
Activity regulationi
Kineticsi
- KM=71 µM for myo-inositol phosphate1 Publication
- KM=64 µM for 1D-myo-inositol 1-phosphate1 Publication
- KM=79 µM for 1D-myo-inositol 3-phosphate1 Publication
- KM=69 µM for myo-inositol phosphate1 Publication
- KM=92 µM for myo-inositol phosphate after 5 minutes at 70 degrees Celsius1 Publication
- KM=110 µM for 1D-myo-inositol 1-phosphate1 Publication
- Vmax=12.3 µmol/min/mg enzyme1 Publication
- Vmax=6.9 µmol/min/mg enzyme for 1D-myo-inositol 1-phosphate1 Publication
- Vmax=2.66 µmol/min/mg enzyme for 1D-myo-inositol 3-phosphate1 Publication
- Vmax=3.38 µmol/min/mg enzyme for myo-inositol phosphate1 Publication
- Vmax=27.6 µmol/min/mg enzyme for myo-inositol phosphate after 5 minutes at 70 degrees Celsius1 Publication
pH dependencei
Temperature dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 67 | Magnesium2 Publications | 1 | |
Binding sitei | 67 | SubstrateBy similarity | 1 | |
Metal bindingi | 84 | Magnesium2 Publications | 1 | |
Metal bindingi | 86 | Magnesium; via carbonyl oxygen2 Publications | 1 | |
Binding sitei | 183 | SubstrateBy similarity | 1 | |
Binding sitei | 212 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- glycerol-2-phosphatase activity Source: EcoCyc
- inositol monophosphate 1-phosphatase activity Source: EcoliWiki
- inositol monophosphate 3-phosphatase activity Source: UniProtKB-EC
- inositol monophosphate 4-phosphatase activity Source: UniProtKB-EC
- lithium ion binding Source: EcoliWiki
- magnesium ion binding Source: EcoliWiki
- RNA binding Source: UniProtKB-KW
GO - Biological processi
- inositol metabolic process Source: GO_Central
- inositol phosphate dephosphorylation Source: EcoliWiki
- phosphatidylinositol phosphorylation Source: InterPro
- ribosome biogenesis Source: UniProtKB-KW
- signal transduction Source: GO_Central
- transcription antitermination Source: UniProtKB-KW
Keywordsi
Molecular function | Chaperone, Hydrolase, RNA-binding |
Biological process | Ribosome biogenesis, Transcription, Transcription antitermination, Transcription regulation |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10983-MONOMER MetaCyc:EG10983-MONOMER |
BRENDAi | 3.1.3.25, 2026 |
SABIO-RKi | P0ADG4 |
Names & Taxonomyi
Protein namesi | Recommended name: Nus factor SuhB1 PublicationAlternative 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 |
Gene namesi | Name:suhB1 Publication Synonyms:ssyA1 Publication Ordered Locus Names:b2533, JW2517 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 87 | D → N: Loss of IMPase activity, still complements dnaB121 helicase mutation. 1 Publication | 1 | |
Mutagenesisi | 139 | R → C in suhB10; decreases polypeptide chain elongation rate, grows at 30 but not 25 degrees Celsius; when associated with A-250. 1 Publication | 1 | |
Mutagenesisi | 173 | G → V: No growth at 30 degrees Celsius, IMPase activity not inhibited by RNA polymerase (RNAP). 1 Publication | 1 | |
Mutagenesisi | 183 | R → A: Some growth at 30 degrees Celsius, greater IMPase activity, partially inhibited by RNAP. 1 Publication | 1 | |
Mutagenesisi | 184 | R → A: Grows at 30 degrees Celsius, makes more dimer, partially inhibited by RNAP, crystallizes. 1 Publication | 1 | |
Mutagenesisi | 184 | R → I: No growth at 30 degrees Celsius, IMPase activity not inhibited by RNAP. 1 Publication | 1 | |
Mutagenesisi | 250 | V → A in suhB10; decreases polypeptide chain elongation rate, grows at 30 but not 25 degrees Celsius; when associated with C-139. 1 Publication | 1 | |
Mutagenesisi | 251 – 254 | KAML → AAMA: 3-fold decreased affinity for NusA, less efficient in delaying or suppressing Rho-dependent transcription termination. 1 Publication | 4 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000142559 | 1 – 267 | Nus factor SuhBAdd BLAST | 267 |
Proteomic databases
jPOSTi | P0ADG4 |
PaxDbi | P0ADG4 |
PRIDEi | P0ADG4 |
2D gel databases
SWISS-2DPAGEi | P0ADG4 |
Expressioni
Inductioni
Interactioni
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 PublicationsProtein-protein interaction databases
BioGRIDi | 4260600, 8 interactors 851613, 5 interactors |
IntActi | P0ADG4, 10 interactors |
STRINGi | 511145.b2533 |
Structurei
Secondary structure
3D structure databases
SMRi | P0ADG4 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0ADG4 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 86 – 89 | Substrate bindingBy similarity | 4 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0483, Bacteria |
HOGENOMi | CLU_044118_0_4_6 |
InParanoidi | P0ADG4 |
PhylomeDBi | P0ADG4 |
Family and domain databases
CDDi | cd01639, IMPase, 1 hit |
InterProi | View protein in InterPro IPR033942, IMPase IPR020583, Inositol_monoP_metal-BS IPR000760, Inositol_monophosphatase-like IPR020550, Inositol_monophosphatase_CS IPR022337, Inositol_monophosphatase_SuhB |
Pfami | View protein in Pfam PF00459, Inositol_P, 1 hit |
PRINTSi | PR00377, IMPHPHTASES PR01959, SBIMPHPHTASE |
PROSITEi | View protein in PROSITE PS00629, IMP_1, 1 hit PS00630, IMP_2, 1 hit |
i Sequence
Sequence statusi: Complete.
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 141 | R → L in AAA67506 (PubMed:2138605).Curated | 1 |
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 |
PIRi | D65030 |
RefSeqi | NP_417028.1, NC_000913.3 WP_000553451.1, NZ_STEB01000011.1 |
Genome annotation databases
EnsemblBacteriai | AAC75586; AAC75586; b2533 BAA16427; BAA16427; BAA16427 |
GeneIDi | 58460715 947285 |
KEGGi | ecj:JW2517 eco:b2533 |
PATRICi | fig|1411691.4.peg.4201 |
Similar proteinsi
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 |
PIRi | D65030 |
RefSeqi | NP_417028.1, NC_000913.3 WP_000553451.1, NZ_STEB01000011.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2QFL | X-ray | 1.90 | A | 1-267 | [»] | |
6IB7 | X-ray | 2.25 | A | 1-267 | [»] | |
6IB8 | X-ray | 1.65 | A/B | 1-267 | [»] | |
6TQN | electron microscopy | 3.80 | S/T | 1-267 | [»] | |
6TQO | electron microscopy | 4.00 | S/T | 1-267 | [»] | |
SMRi | P0ADG4 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260600, 8 interactors 851613, 5 interactors |
IntActi | P0ADG4, 10 interactors |
STRINGi | 511145.b2533 |
2D gel databases
SWISS-2DPAGEi | P0ADG4 |
Proteomic databases
jPOSTi | P0ADG4 |
PaxDbi | P0ADG4 |
PRIDEi | P0ADG4 |
Genome annotation databases
EnsemblBacteriai | AAC75586; AAC75586; b2533 BAA16427; BAA16427; BAA16427 |
GeneIDi | 58460715 947285 |
KEGGi | ecj:JW2517 eco:b2533 |
PATRICi | fig|1411691.4.peg.4201 |
Organism-specific databases
EchoBASEi | EB0976 |
Phylogenomic databases
eggNOGi | COG0483, Bacteria |
HOGENOMi | CLU_044118_0_4_6 |
InParanoidi | P0ADG4 |
PhylomeDBi | P0ADG4 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10983-MONOMER MetaCyc:EG10983-MONOMER |
BRENDAi | 3.1.3.25, 2026 |
SABIO-RKi | P0ADG4 |
Miscellaneous databases
EvolutionaryTracei | P0ADG4 |
PROi | PR:P0ADG4 |
Family and domain databases
CDDi | cd01639, IMPase, 1 hit |
InterProi | View protein in InterPro IPR033942, IMPase IPR020583, Inositol_monoP_metal-BS IPR000760, Inositol_monophosphatase-like IPR020550, Inositol_monophosphatase_CS IPR022337, Inositol_monophosphatase_SuhB |
Pfami | View protein in Pfam PF00459, Inositol_P, 1 hit |
PRINTSi | PR00377, IMPHPHTASES PR01959, SBIMPHPHTASE |
PROSITEi | View protein in PROSITE PS00629, IMP_1, 1 hit PS00630, IMP_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SUHB_ECOLI | |
Accessioni | P0ADG4Primary (citable) accession number: P0ADG4 Secondary accession number(s): P22783, P77511, Q8X2E6 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families