ID   SUHB_BUCAI              Reviewed;         266 AA.
AC   P57372;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=BU285;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB12995.1; -; Genomic_DNA.
DR   RefSeq; NP_240109.1; NC_002528.1.
DR   RefSeq; WP_009874239.1; NC_002528.1.
DR   AlphaFoldDB; P57372; -.
DR   SMR; P57372; -.
DR   STRING; 107806.10038960; -.
DR   EnsemblBacteria; BAB12995; BAB12995; BAB12995.
DR   KEGG; buc:BU285; -.
DR   PATRIC; fig|107806.10.peg.295; -.
DR   eggNOG; COG0483; Bacteria.
DR   HOGENOM; CLU_044118_0_0_6; -.
DR   OMA; CLAIIED; -.
DR   Proteomes; UP000001806; 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   InterPro; IPR022337; Inositol_monophosphatase_SuhB.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PRINTS; PR01959; SBIMPHPHTASE.
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_0000142555"
FT   BINDING         87..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  30568 MW;  413FA9CEDDB41950 CRC64;
     MHPMLNIAIR AVRKGGNFII QNYERRKFVK EDVEKNKVFL NNIIYKTNKI ISEIIHKSYP
     YHTILKKHEN ILVKKNEKNT VWIITELDGK TNFLKYFPYF CVSIAVVVKN KTEISVIYDP
     IKNDLFTAVK GQGSQLNGYR TRCSAINTLN YSTVAVNPSN KIHNLTSSYF EIYKKLIISG
     ISFRCTGSSI LDSAYVAAGK IDCLFDFNLD PNKFVASKLQ VREAGCLINN FMGEYEHNNN
     NYSGNITSSS KFIRLINEKI RECYLI