SUHB_BUCBP
ID SUHB_BUCBP Reviewed; 266 AA.
AC Q89AK9;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Nus factor SuhB {ECO:0000250|UniProtKB:P0ADG4};
DE AltName: Full=Inositol-1-monophosphatase;
DE Short=I-1-Pase;
DE Short=IMPase;
DE Short=Inositol-1-phosphatase;
DE EC=3.1.3.25 {ECO:0000250|UniProtKB:P0ADG4};
GN Name=suhB; OrderedLocusNames=bbp_264;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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. {ECO:0000250|UniProtKB:P0ADG4}.
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:0000250|UniProtKB:P0ADG4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0ADG4};
CC -!- SUBUNIT: Homodimer. 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. {ECO:0000250|UniProtKB:P0ADG4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0ADG4}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE016826; AAO26990.1; -; Genomic_DNA.
DR RefSeq; WP_011091391.1; NC_004545.1.
DR AlphaFoldDB; Q89AK9; -.
DR SMR; Q89AK9; -.
DR STRING; 224915.bbp_264; -.
DR EnsemblBacteria; AAO26990; AAO26990; bbp_264.
DR GeneID; 56470806; -.
DR KEGG; bab:bbp_264; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_0_6; -.
DR OMA; VHQELEF; -.
DR OrthoDB; 1741160at2; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-KW.
DR CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Hydrolase; Reference proteome; Ribosome biogenesis;
KW RNA-binding; Transcription; Transcription antitermination;
KW Transcription regulation.
FT CHAIN 1..266
FT /note="Nus factor SuhB"
FT /id="PRO_0000142557"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 266 AA; 30496 MW; 4C4166EB634D556A CRC64;
MHPILNIAIR VARKCGNILI QYYDRNKTNN EKQILKKDFI TKIIFVLEKT MIDMIHKSYP
EHSIITYHKN NKIFKNTEII WLINALDGIK NFENNLPHFC ISIAIIVRKT TQISVIYDPI
RNELFTSVKG QGSQLNGYRM RCKSTNTLKR SLVGLVYPCN NSKFQNYFFT IINLLFSHEV
KLRCTGCISL DCAYVAMGRL DYLFNGNLIP LLFSSGSLQI KESGGLISDL NGGHDYVSSG
IILIGNPKLM RVILVKIREL FQNNLK