SUHB_NEIMA
ID SUHB_NEIMA Reviewed; 261 AA.
AC Q9JU03; A1ISE8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative Nus factor SuhB {ECO:0000250|UniProtKB:B4ED80};
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=NMA1559;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
CC -!- FUNCTION: Might be 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. {ECO:0000250|UniProtKB:B4ED80,
CC 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; AL157959; CAM08704.1; -; Genomic_DNA.
DR PIR; B81848; B81848.
DR RefSeq; WP_002237077.1; NC_003116.1.
DR AlphaFoldDB; Q9JU03; -.
DR SMR; Q9JU03; -.
DR EnsemblBacteria; CAM08704; CAM08704; NMA1559.
DR KEGG; nma:NMA1559; -.
DR HOGENOM; CLU_044118_0_4_4; -.
DR OMA; VHQELEF; -.
DR BioCyc; NMEN122587:NMA_RS07785-MON; -.
DR Proteomes; UP000000626; 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 Ribosome biogenesis; RNA-binding; Transcription;
KW Transcription antitermination; Transcription regulation.
FT CHAIN 1..261
FT /note="Putative Nus factor SuhB"
FT /id="PRO_0000142566"
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 261 AA; 28497 MW; 23DCA23F3DD63734 CRC64;
MNPFLNTAFK AARRAGQMMI RAAGNLDAVK TDSKAFNDFV SDVDRNSEII LVEALKEAYP
HHKITCEESG SHGKAAAEYE WIIDPLDGTT NFLHGHPQYA ISMALLHKGV LQEALVYAPE
RNDVYMASRG KGALLNDRRI RVSNRIELNR CLIGTGFPVV DQSMMDKYLV ILKDFLAKTA
GGRREGAASL DLCAVATGRF DGFFEFNLKP WDIAAGALIV QEAGGIVTDM SGEDGWLESG
DIVAANPKVL AQMLKIISAH V
