ID   SUHB_BUCAP              Reviewed;         269 AA.
AC   Q8K9P6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=BUsg_274;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67832.1; -; Genomic_DNA.
DR   RefSeq; WP_011053799.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9P6; -.
DR   SMR; Q8K9P6; -.
DR   STRING; 198804.BUsg_274; -.
DR   PRIDE; Q8K9P6; -.
DR   EnsemblBacteria; AAM67832; AAM67832; BUsg_274.
DR   KEGG; bas:BUsg_274; -.
DR   eggNOG; COG0483; Bacteria.
DR   HOGENOM; CLU_044118_0_0_6; -.
DR   OMA; VHQELEF; -.
DR   OrthoDB; 1741160at2; -.
DR   Proteomes; UP000000416; 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; Ribosome biogenesis; RNA-binding;
KW   Transcription; Transcription antitermination; Transcription regulation.
FT   CHAIN           1..269
FT                   /note="Nus factor SuhB"
FT                   /id="PRO_0000142556"
FT   BINDING         85..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   269 AA;  30842 MW;  7105600E0D8E9A6B CRC64;
     MHPMLNIAIR AIRKGGNIIV QNYDTQKFIK EDLDKKKIFI KNIMYKTYRI ISEVIYKSYP
     NHIILNKNTD LIKNEKNTLW IINELDGKNN FIKNFPHFCI SIAVIMKNNT EISVIYDPIR
     NDLFTAVKGQ GSQLNGYRIR CNNINSLNYS TIAINLPLKH YAKSLFYLKI YKKLILSGIS
     LRCTGSTLLD LAYVASGRID CLFDFNPQSI NLIAGKLQAR EAGCLTSKFT ENSEKKSEKG
     NFCTSNLTSS SKFMRLITEK ISQCYSFNN