SUHB_SALT1
ID SUHB_SALT1 Reviewed; 267 AA.
AC A0A0F6B4W4;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 30.
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=STM14_3124;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP FUNCTION, SUBUNIT, AND PROBABLE INDUCTION.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=29229908; DOI=10.1038/s41467-017-02124-9;
RA Baniulyte G., Singh N., Benoit C., Johnson R., Ferguson R., Paramo M.,
RA Stringer A.M., Scott A., Lapierre P., Wade J.T.;
RT "Identification of regulatory targets for the bacterial Nus factor
RT complex.";
RL Nat. Commun. 8:2027-2027(2017).
CC -!- FUNCTION: Associates with the boxA element in its own promoter
CC (PubMed:29229908). Part of the processive rRNA transcription and
CC antitermination complex (rrnTAC). The complex forms an RNA-chaperone
CC ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports
CC rapid transcription and antitermination of rRNA operons,
CC cotranscriptional rRNA folding, and annealing of distal rRNA regions to
CC allow correct ribosome biogenesis. This subunit may play a central role
CC in organizing the structure (By similarity).
CC {ECO:0000250|UniProtKB:P0ADG4, ECO:0000269|PubMed:29229908}.
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 -!- INDUCTION: Repressed by the Nus factor complex (NusA, NusB, NusE
CC (rpsJ), NusG and SuhB). {ECO:0000305|PubMed:29229908}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; CP001363; ACY89555.1; -; Genomic_DNA.
DR RefSeq; WP_000553467.1; NZ_CP043402.1.
DR AlphaFoldDB; A0A0F6B4W4; -.
DR SMR; A0A0F6B4W4; -.
DR EnsemblBacteria; ACY89555; ACY89555; STM14_3124.
DR KEGG; seo:STM14_3124; -.
DR PATRIC; fig|588858.6.peg.2897; -.
DR HOGENOM; CLU_044118_0_4_6; -.
DR OMA; RVDGYWE; -.
DR BioCyc; SENT588858:STM14_RS13955-MON; -.
DR Proteomes; UP000002695; 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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Ribosome biogenesis; RNA-binding; Transcription;
KW Transcription antitermination; Transcription regulation.
FT CHAIN 1..267
FT /note="Nus factor SuhB"
FT /id="PRO_0000451746"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
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
