ID SUHB_SALTY Reviewed; 267 AA. AC P58537; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 1. DT 04-NOV-2026, entry version 123. 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=STM2546; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(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; AE006468; AAL21440.1; -; Genomic_DNA. DR RefSeq; NP_461481.1; NC_003197.2. DR RefSeq; WP_000553467.1; NC_003197.2. DR SMR; P58537; -. DR STRING; 99287.STM2546; -. DR PaxDb; 99287-STM2546; -. DR GeneID; 1254068; -. DR KEGG; stm:STM2546; -. DR PATRIC; fig|99287.12.peg.2686; -. DR HOGENOM; CLU_044118_0_4_6; -. DR OMA; AAAMNMC; -. DR PhylomeDB; P58537; -. DR BioCyc; SENT99287:STM2546-MONOMER; -. DR CDD; cd01639; IMPase; 1. DR FunFam; 3.30.540.10:FF:000003; Inositol-1-monophosphatase; 1. DR FunFam; 3.40.190.80:FF:000004; Inositol-1-monophosphatase; 1. DR Gene3D; 3.40.190.80; -; 1. DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 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 PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1. DR PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR PRINTS; PR01959; SBIMPHPHTASE. DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1. DR NCBIfam; NF008027; suhB; 1. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central. DR GO; GO:0052834; F:inositol monophosphate phosphatase activity; ISS:UniProtKB. DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central. DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR Proteomes; UP000001014; Chromosome. DR AlphaFoldDB; P58537; -. 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_0000142572" 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; 29158 MW; FC46D8A8298BB334 CRC64; MHPMLTIAVR AARKAGNVIA KNYETPDAVE ASQKGSNDFV TNVDKAAEAV IIDTIRKSYP QHTIITEESG EHVGTDQDVQ WVIDPLDGTT NFIKRLPHFA VSIAVRIKGR TEVAVVYDPM RNELFTATRG QGAQLNGYRL RGSTARDLDG TILATGFPFK AKQYATTYIN IIGKLFTECA DFRRTGSAAL DLAYVAAGRV DGFFEIGLRP WDFAAGELLV REAGGIVSDF TGGHNYMMTG NIVAGNPRVV KAMLANMRDE LSDALKR //