SUHB_ECOLI
ID SUHB_ECOLI Reviewed; 267 AA.
AC P0ADG4; P22783; P77511; Q8X2E6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Nus factor SuhB {ECO:0000303|PubMed:32871103};
DE AltName: Full=Inositol-1-monophosphatase {ECO:0000303|PubMed:8002619};
DE Short=I-1-Pase {ECO:0000303|PubMed:10747806};
DE Short=IMPase;
DE Short=Inositol-1-phosphatase;
DE EC=3.1.3.25 {ECO:0000269|PubMed:8002619};
GN Name=suhB {ECO:0000303|PubMed:2138605};
GN Synonyms=ssyA {ECO:0000303|PubMed:6389495};
GN OrderedLocusNames=b2533, JW2517;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS A SUPPRESSOR OF RPOH
RP MISSENSE MUTATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2138605; DOI=10.1128/jb.172.4.2124-2130.1990;
RA Yano R., Nagai H., Shiba K., Yura T.;
RT "A mutation that enhances synthesis of sigma 32 and suppresses temperature-
RT sensitive growth of the rpoH15 mutant of Escherichia coli.";
RL J. Bacteriol. 172:2124-2130(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION AS A SUPPRESSOR OF SECY TEMPERATURE-SENSITIVE MUTATION.
RC STRAIN=K12;
RX PubMed=6389495; DOI=10.1128/jb.160.2.696-701.1984;
RA Shiba K., Ito K., Yura T.;
RT "Mutation that suppresses the protein export defect of the secY mutation
RT and causes cold-sensitive growth of Escherichia coli.";
RL J. Bacteriol. 160:696-701(1984).
RN [6]
RP SUBSTRATE LEVELS IN E.COLI.
RC STRAIN=K12 / HB101;
RX PubMed=1848220; DOI=10.1128/jb.173.6.2053-2060.1991;
RA Kozloff L.M., Turner M.A., Arellano F., Lute M.;
RT "Phosphatidylinositol, a phospholipid of ice-nucleating bacteria.";
RL J. Bacteriol. 173:2053-2060(1991).
RN [7]
RP FUNCTION AS A SUPPRESSOR OF DNAB MISSENSE MUTATION.
RC STRAIN=K12 / W3110 / B178;
RX PubMed=1847383; DOI=10.1016/s0021-9258(19)67844-0;
RA Chang S.F., Ng D., Baird L., Georgopoulos C.;
RT "Analysis of an Escherichia coli dnaB temperature-sensitive insertion
RT mutation and its cold-sensitive extragenic suppressor.";
RL J. Biol. Chem. 266:3654-3660(1991).
RN [8]
RP FUNCTION AS AN INOSITOL MONOPHOSPHATASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8002619; DOI=10.1128/jb.177.1.200-205.1995;
RA Matsuhisa A., Suzuki N., Noda T., Shiba K.;
RT "Inositol monophosphatase activity from the Escherichia coli suhB gene
RT product.";
RL J. Bacteriol. 177:200-205(1995).
RN [9]
RP GENETIC ANALYSIS, AND MUTAGENESIS OF ARG-139 AND VAL-250.
RC STRAIN=K12;
RX PubMed=8589060; DOI=10.1016/0300-9084(96)88139-9;
RA Inada T., Nakamura Y.;
RT "Lethal double-stranded RNA processing activity of ribonuclease III in the
RT absence of suhB protein of Escherichia coli.";
RL Biochimie 77:294-302(1995).
RN [10]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=8831954; DOI=10.1016/0300-9084(96)89508-3;
RA Inada T., Nakamura Y.;
RT "Autogenous control of the suhB gene expression of Escherichia coli.";
RL Biochimie 78:209-212(1996).
RN [11]
RP FUNCTION AS AN INOSITOL MONOPHOSPHATASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-87.
RX PubMed=10747806; DOI=10.1021/bi992424f;
RA Chen L., Roberts M.F.;
RT "Overexpression, purification, and analysis of complementation behavior of
RT E. coli SuhB protein: comparison with bacterial and archaeal inositol
RT monophosphatases.";
RL Biochemistry 39:4145-4153(2000).
RN [12]
RP ACTIVITY REGULATION.
RX PubMed=22384802; DOI=10.1021/ja211794x;
RA Haimovich A., Eliav U., Goldbourt A.;
RT "Determination of the lithium binding site in inositol monophosphatase, the
RT putative target for lithium therapy, by magic-angle-spinning solid-state
RT NMR.";
RL J. Am. Chem. Soc. 134:5647-5651(2012).
RN [13]
RP FUNCTION IN RRNA MATURATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076, and K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=26980831; DOI=10.1128/mbio.00114-16;
RA Singh N., Bubunenko M., Smith C., Abbott D.M., Stringer A.M., Shi R.,
RA Court D.L., Wade J.T.;
RT "SuhB Associates with Nus Factors To Facilitate 30S Ribosome Biogenesis in
RT Escherichia coli.";
RL MBio 7:e00114-e00114(2016).
RN [14]
RP FUNCTION IN GENE REGULATION, SUBUNIT, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=29229908; DOI=10.1038/s41467-017-02124-9;
RA Baniulyte G., Singh N., Benoit C., Johnson R., Ferguson R., Paramo M.,
RA Stringer A.M., Scott A., Lapierre P., Wade J.T.;
RT "Identification of regulatory targets for the bacterial Nus factor
RT complex.";
RL Nat. Commun. 8:2027-2027(2017).
RN [15]
RP INTERACTION WITH NUSA, AND PRECURSOR RRNA-BINDING.
RX PubMed=31127279; DOI=10.1093/nar/gkz442;
RA Dudenhoeffer B.R., Schneider H., Schweimer K., Knauer S.H.;
RT "SuhB is an integral part of the ribosomal antitermination complex and
RT interacts with NusA.";
RL Nucleic Acids Res. 47:6504-6518(2019).
RN [16] {ECO:0007744|PDB:2QFL}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH RNA POLYMERASE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-173; ARG-183 AND ARG-184.
RX PubMed=17652087; DOI=10.1074/jbc.m701210200;
RA Wang Y., Stieglitz K.A., Bubunenko M., Court D.L., Stec B., Roberts M.F.;
RT "The structure of the R184A mutant of the inositol monophosphatase encoded
RT by suhB and implications for its functional interactions in Escherichia
RT coli.";
RL J. Biol. Chem. 282:26989-26996(2007).
RN [17] {ECO:0007744|PDB:6IB7, ECO:0007744|PDB:6IB8}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH MG(2+) ALONE AND IN
RP COMPLEX WITH NUSA, COFACTOR, SUBUNIT, INTERACTION WITH NUSA, PRECURSOR
RP RRNA-BINDING, AND MUTAGENESIS OF 251-LYS--LEU-254.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=31020314; DOI=10.1093/nar/gkz290;
RA Huang Y.H., Said N., Loll B., Wahl M.C.;
RT "Structural basis for the function of SuhB as a transcription factor in
RT ribosomal RNA synthesis.";
RL Nucleic Acids Res. 47:6488-6503(2019).
RN [18] {ECO:0007744|PDB:6TQN, ECO:0007744|PDB:6TQO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RRNA
RP TRANSCRIPTION-ELONGATION-ANTITERMINATION COMPLEXES WITH AND WITHOUT S4,
RP FUNCTION, SUBUNIT, AND COFACTOR.
RX PubMed=32871103; DOI=10.1016/j.molcel.2020.08.010;
RA Huang Y.H., Hilal T., Loll B., Buerger J., Mielke T., Boettcher C.,
RA Said N., Wahl M.C.;
RT "Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine
RT Required for Ribosome Biosynthesis.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: Part of the processive rRNA transcription and antitermination
CC complex (rrnTAC). The complex forms an RNA-chaperone ring around the
CC RNA exit tunnel of RNA polymerase (RNAP). It supports rapid
CC transcription and antitermination of rRNA operons, cotranscriptional
CC rRNA folding, and annealing of distal rRNA regions to allow correct
CC ribosome biogenesis. This subunit may play a central role in organizing
CC the structure (PubMed:32871103). Involved in 30S ribosomal subunit
CC biogenesis; thought to be required for loop formation between NusB/NusE
CC (rpsJ, ribosomal protein S10) bound to boxA upstream of the rRNA
CC operons and the elongating RNAP complex. This would promote correct co-
CC transcriptional folding of rRNA. Plays a role in transcription
CC antitermination in a plasmid context in vivo (PubMed:26980831).
CC Required for rrn transcription antitermination; required for
CC integration of NusB/NusE into the antitermination complex
CC (PubMed:31020314). The Nus factor complex (NusA, NusB, NusE (rpsJ),
CC NusG and SuhB) represses expression of suhB and possibly other genes
CC via boxA; the Nus complex prevents or promotes Rho-mediated
CC transcription termination depending on gene context (PubMed:29229908).
CC Involved in post-transcriptional control of gene expression (Probable).
CC Enzymatic activity is not required for complementation of the cold-
CC sensitive phenotype of the dnaB121 mutation (PubMed:10747806)
CC (Probable). {ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:26980831,
CC ECO:0000269|PubMed:29229908, ECO:0000269|PubMed:31020314,
CC ECO:0000269|PubMed:32871103, ECO:0000305|PubMed:17652087,
CC ECO:0000305|PubMed:1847383, ECO:0000305|PubMed:2138605,
CC ECO:0000305|PubMed:6389495, ECO:0000305|PubMed:8589060,
CC ECO:0000305|PubMed:8831954}.
CC -!- FUNCTION: Has D,L-inositol-1-monophosphatase and beta-
CC glycerophosphatase activity, has less to no activity against a number
CC of other substrates (PubMed:8002619). 2.5-fold more active on 1D-
CC inositol-1-monophosphate than L-inositol-1-monophosphate (1D-myo-
CC inositol 3-phosphate). Specific activity increases significantly upon
CC heating. Only beta-glycerophosphate and adenosine 2'-monophosphate are
CC alternative substrates (PubMed:10747806). {ECO:0000269|PubMed:10747806,
CC ECO:0000269|PubMed:8002619}.
CC -!- FUNCTION: Required for growth at low temperatures (PubMed:2138605,
CC PubMed:6389495, PubMed:1847383, PubMed:8002619, PubMed:8589060,
CC PubMed:17652087, PubMed:26980831). Identified as a suppressor (ssyA3)
CC of a temperature-sensitive, protein export missense mutation of secY
CC (secY24), allows growth at 42 but not 30 degrees Celsius
CC (PubMed:6389495). Identified as a suppressor (suhB2) of an rpoH
CC missense mutation (rpoH15), allowing growth at 37 and 40 but not 25, 30
CC or 34 degrees Celsius, increases expression of RpoH (PubMed:2138605).
CC Identified as a suppressor of a dnaB helicase missense mutation
CC (dnaB121), restores growth at 42 but not 30 degrees Celsius
CC (PubMed:1847383). In both suhB2 and ssyA3 there is an insertion in the
CC 5' region of the gene which prevents SuhB protein expression
CC (PubMed:8002619, PubMed:8589060). Missense mutant suhB10 is suppressed
CC by mutations in RNase III (rnc), showing genetic interaction between
CC them (PubMed:8589060). Deletion of suhB is suppressed by mutations in
CC RNase III, by a mutation in nusA or deletion of nusB, indicating that
CC in the absence of SuhB the Nus complex inhibits growth
CC (PubMed:26980831). {ECO:0000269|PubMed:17652087,
CC ECO:0000269|PubMed:1847383, ECO:0000269|PubMed:2138605,
CC ECO:0000269|PubMed:26980831, ECO:0000269|PubMed:6389495,
CC ECO:0000269|PubMed:8002619, ECO:0000269|PubMed:8589060}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:8002619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1-phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:27670, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58433; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:17652087};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:30739, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58401; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:10747806};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:31020314,
CC ECO:0000269|PubMed:32871103, ECO:0000269|PubMed:8002619};
CC Note=Partial activity is seen with Co(2+), Ni(2+), Mn(2+), Zn(2+) and
CC Fe(2+); in the presence of Mg(2+) these cations inhibit.
CC {ECO:0000269|PubMed:10747806};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+) (PubMed:8002619,
CC PubMed:10747806) (Probable). Li(+) binds to Asp-84, Asp-87 and Asp-212
CC (PubMed:22384802). {ECO:0000269|PubMed:10747806,
CC ECO:0000269|PubMed:22384802, ECO:0000269|PubMed:8002619,
CC ECO:0000305|PubMed:22384802}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=71 uM for myo-inositol phosphate {ECO:0000269|PubMed:8002619};
CC KM=64 uM for 1D-myo-inositol 1-phosphate
CC {ECO:0000269|PubMed:10747806};
CC KM=79 uM for 1D-myo-inositol 3-phosphate
CC {ECO:0000269|PubMed:10747806};
CC KM=69 uM for myo-inositol phosphate {ECO:0000269|PubMed:10747806};
CC KM=92 uM for myo-inositol phosphate after 5 minutes at 70 degrees
CC Celsius {ECO:0000269|PubMed:10747806};
CC KM=110 uM for 1D-myo-inositol 1-phosphate
CC {ECO:0000269|PubMed:17652087};
CC Vmax=12.3 umol/min/mg enzyme {ECO:0000269|PubMed:8002619};
CC Vmax=6.9 umol/min/mg enzyme for 1D-myo-inositol 1-phosphate
CC {ECO:0000269|PubMed:10747806};
CC Vmax=2.66 umol/min/mg enzyme for 1D-myo-inositol 3-phosphate
CC {ECO:0000269|PubMed:10747806};
CC Vmax=3.38 umol/min/mg enzyme for myo-inositol phosphate
CC {ECO:0000269|PubMed:10747806};
CC Vmax=27.6 umol/min/mg enzyme for myo-inositol phosphate after 5
CC minutes at 70 degrees Celsius {ECO:0000269|PubMed:10747806};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:8002619};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius, 90% of activity remains
CC after heating at 70 degrees Celsius for 5 minutes.
CC {ECO:0000269|PubMed:10747806};
CC -!- SUBUNIT: Monomer (PubMed:10747806, PubMed:31127279). A monomer-dimer
CC equilibrium (PubMed:17652087). Homodimer (PubMed:31020314,
CC PubMed:32871103). The rRNA transcription and antitermination complex
CC (rrnTAC) consists of RNA polymerase (RNAP), NusA, NusB, NusE (rpsJ),
CC NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is more
CC flexible than other subunits (PubMed:31127279, PubMed:31020314,
CC PubMed:32871103). Binds to RNAP, which decreases IMPase activity
CC against 1D-myo-inositol 1-phosphate (PubMed:17652087) (Probable).
CC Association with rRNA gene-transcribing RNAP is dependent on NusB
CC (PubMed:26980831, PubMed:29229908). Interacts with AR2 domain of NusA;
CC crystallizes as a 2:1 SuhB:NusA heterotrimer (PubMed:31020314,
CC PubMed:31127279). {ECO:0000269|PubMed:10747806,
CC ECO:0000269|PubMed:17652087, ECO:0000269|PubMed:26980831,
CC ECO:0000269|PubMed:29229908, ECO:0000269|PubMed:31020314,
CC ECO:0000269|PubMed:31127279, ECO:0000269|PubMed:32871103,
CC ECO:0000305|PubMed:31127279}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10747806}.
CC -!- INDUCTION: Transcription is autoregulated (PubMed:8831954). Repressed
CC by the Nus factor complex (NusA, NusB, NusE (rpsJ), NusG and SuhB)
CC (PubMed:29229908). {ECO:0000269|PubMed:29229908,
CC ECO:0000269|PubMed:8831954}.
CC -!- DISRUPTION PHENOTYPE: Conditionally lethal, cells are unable to grow at
CC 30 degrees Celsius and less, grow poorly at 37 degrees Celsius, but do
CC grow at 42 degrees Celsius. {ECO:0000269|PubMed:17652087,
CC ECO:0000269|PubMed:26980831}.
CC -!- MISCELLANEOUS: E.coli makes very low amounts of myo-inositol-containing
CC phospholipids, so the catalytic necessity for this enzyme is low.
CC {ECO:0000305|PubMed:17652087, ECO:0000305|PubMed:1848220}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; M34828; AAA67506.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75586.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16427.1; -; Genomic_DNA.
DR PIR; D65030; D65030.
DR RefSeq; NP_417028.1; NC_000913.3.
DR RefSeq; WP_000553451.1; NZ_STEB01000011.1.
DR PDB; 2QFL; X-ray; 1.90 A; A=1-267.
DR PDB; 6IB7; X-ray; 2.25 A; A=1-267.
DR PDB; 6IB8; X-ray; 1.65 A; A/B=1-267.
DR PDB; 6TQN; EM; 3.80 A; S/T=1-267.
DR PDB; 6TQO; EM; 4.00 A; S/T=1-267.
DR PDBsum; 2QFL; -.
DR PDBsum; 6IB7; -.
DR PDBsum; 6IB8; -.
DR PDBsum; 6TQN; -.
DR PDBsum; 6TQO; -.
DR AlphaFoldDB; P0ADG4; -.
DR SMR; P0ADG4; -.
DR BioGRID; 4260600; 8.
DR BioGRID; 851613; 5.
DR IntAct; P0ADG4; 10.
DR STRING; 511145.b2533; -.
DR SWISS-2DPAGE; P0ADG4; -.
DR jPOST; P0ADG4; -.
DR PaxDb; P0ADG4; -.
DR PRIDE; P0ADG4; -.
DR EnsemblBacteria; AAC75586; AAC75586; b2533.
DR EnsemblBacteria; BAA16427; BAA16427; BAA16427.
DR GeneID; 66673579; -.
DR GeneID; 947285; -.
DR KEGG; ecj:JW2517; -.
DR KEGG; eco:b2533; -.
DR PATRIC; fig|1411691.4.peg.4201; -.
DR EchoBASE; EB0976; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_4_6; -.
DR InParanoid; P0ADG4; -.
DR OMA; RVDGYWE; -.
DR PhylomeDB; P0ADG4; -.
DR BioCyc; EcoCyc:EG10983-MON; -.
DR BioCyc; MetaCyc:EG10983-MON; -.
DR BRENDA; 3.1.3.25; 2026.
DR SABIO-RK; P0ADG4; -.
DR EvolutionaryTrace; P0ADG4; -.
DR PRO; PR:P0ADG4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0047954; F:glycerol-2-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0031403; F:lithium ion binding; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:EcoCyc.
DR GO; GO:0001072; F:transcription antitermination factor activity, RNA binding; IDA:EcoCyc.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:EcoliWiki.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0031564; P:transcription antitermination; IMP:EcoCyc.
DR CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR InterPro; IPR022337; Inositol_monophosphatase_SuhB.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PRINTS; PR01959; SBIMPHPHTASE.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding; Transcription;
KW Transcription antitermination; Transcription regulation.
FT CHAIN 1..267
FT /note="Nus factor SuhB"
FT /id="PRO_0000142559"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31020314,
FT ECO:0000269|PubMed:32871103"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31020314,
FT ECO:0000269|PubMed:32871103"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:31020314,
FT ECO:0000269|PubMed:32871103"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 87
FT /note="D->N: Loss of IMPase activity, still complements
FT dnaB121 helicase mutation."
FT /evidence="ECO:0000269|PubMed:10747806"
FT MUTAGEN 139
FT /note="R->C: In suhB10; decreases polypeptide chain
FT elongation rate, grows at 30 but not 25 degrees Celsius;
FT when associated with A-250."
FT /evidence="ECO:0000269|PubMed:8589060"
FT MUTAGEN 173
FT /note="G->V: No growth at 30 degrees Celsius, IMPase
FT activity not inhibited by RNA polymerase (RNAP)."
FT /evidence="ECO:0000269|PubMed:17652087"
FT MUTAGEN 183
FT /note="R->A: Some growth at 30 degrees Celsius, greater
FT IMPase activity, partially inhibited by RNAP."
FT /evidence="ECO:0000269|PubMed:17652087"
FT MUTAGEN 184
FT /note="R->A: Grows at 30 degrees Celsius, makes more dimer,
FT partially inhibited by RNAP, crystallizes."
FT /evidence="ECO:0000269|PubMed:17652087"
FT MUTAGEN 184
FT /note="R->I: No growth at 30 degrees Celsius, IMPase
FT activity not inhibited by RNAP."
FT /evidence="ECO:0000269|PubMed:17652087"
FT MUTAGEN 250
FT /note="V->A: In suhB10; decreases polypeptide chain
FT elongation rate, grows at 30 but not 25 degrees Celsius;
FT when associated with C-139."
FT /evidence="ECO:0000269|PubMed:8589060"
FT MUTAGEN 251..254
FT /note="KAML->AAMA: 3-fold decreased affinity for NusA, less
FT efficient in delaying or suppressing Rho-dependent
FT transcription termination."
FT /evidence="ECO:0000269|PubMed:31020314"
FT CONFLICT 141
FT /note="R -> L (in Ref. 1; AAA67506)"
FT /evidence="ECO:0000305"
FT HELIX 3..23
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6IB8"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 75..87
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:6IB8"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6IB8"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 247..264
FT /evidence="ECO:0007829|PDB:6IB8"
SQ SEQUENCE 267 AA; 29172 MW; 8FEC3508BD111301 CRC64;
MHPMLNIAVR AARKAGNLIA KNYETPDAVE ASQKGSNDFV TNVDKAAEAV IIDTIRKSYP
QHTIITEESG ELEGTDQDVQ WVIDPLDGTT NFIKRLPHFA VSIAVRIKGR TEVAVVYDPM
RNELFTATRG QGAQLNGYRL RGSTARDLDG TILATGFPFK AKQYATTYIN IVGKLFNECA
DFRRTGSAAL DLAYVAAGRV DGFFEIGLRP WDFAAGELLV REAGGIVSDF TGGHNYMLTG
NIVAGNPRVV KAMLANMRDE LSDALKR
