ID   SUHB_PASMU              Reviewed;         267 AA.
AC   Q9CNV8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=PM0315;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004439; AAK02399.1; -; Genomic_DNA.
DR   RefSeq; WP_005725868.1; NC_002663.1.
DR   AlphaFoldDB; Q9CNV8; -.
DR   SMR; Q9CNV8; -.
DR   STRING; 747.DR93_1089; -.
DR   EnsemblBacteria; AAK02399; AAK02399; PM0315.
DR   GeneID; 62224757; -.
DR   KEGG; pmu:PM0315; -.
DR   PATRIC; fig|272843.6.peg.328; -.
DR   HOGENOM; CLU_044118_0_4_6; -.
DR   OMA; RVDGYWE; -.
DR   Proteomes; UP000000809; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; 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; 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   3: Inferred from homology;
KW   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_0000142568"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADG4"
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:0000250|UniProtKB:P0ADG4"
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:0000250|UniProtKB:P0ADG4"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   267 AA;  29470 MW;  E7070FAE3BA589CA CRC64;
     MNPMLNIAIR AARKAGNVIA KGYERRDDLQ TTLKSTNDYV TNIDKASEEA IIEVIRKSYP
     DHTIITEESG ALEGKDSDIQ WVIDPLDGTT NFVKGLPHFS VSIAIRVKGR TEVGVVYDPI
     RNELFTAVRG EGAKINDMRL RVENKRDLAG TVLTTGFPFK QTRLMPMQFA MMNNLIQDCA
     DFRRMGSAAL DLCYVAAGRV DGYFEVGVKA WDIAAGDLIV REAGGLVCDF NGGHSYLTSG
     HLVAAAPRIV KEILNKIQPC LSDEFKK