SUHB_NEIMB
ID SUHB_NEIMB Reviewed; 261 AA.
AC Q9JZ07;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=NMB1347;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(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; AE002098; AAF41721.1; -; Genomic_DNA.
DR PIR; F81092; F81092.
DR RefSeq; NP_274365.1; NC_003112.2.
DR RefSeq; WP_002222348.1; NC_003112.2.
DR AlphaFoldDB; Q9JZ07; -.
DR SMR; Q9JZ07; -.
DR STRING; 122586.NMB1347; -.
DR PaxDb; Q9JZ07; -.
DR EnsemblBacteria; AAF41721; AAF41721; NMB1347.
DR KEGG; nme:NMB1347; -.
DR PATRIC; fig|122586.8.peg.1686; -.
DR HOGENOM; CLU_044118_0_4_4; -.
DR OMA; VHQELEF; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
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:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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..261
FT /note="Putative Nus factor SuhB"
FT /id="PRO_0000142567"
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; 28469 MW; 3D22B2295AC04653 CRC64;
MNPFLNTAFK AARRAGQMMI RAAGNLDAVK TDSKAFNDFV SDVDRNSEII LVEALKEAYP
HHKITCEESG SHGKAAAEYE WIIDPLDGTT NFLHGHPQYA ISMALLHKGV LQEALVYAPE
RNDVYMASRG KGALLNDRRI RVSNRIELNR CLIGTGFPVV DQSMMDKYLA ILKDFLAKTA
GGRREGAASL DLCAVATGRF DGFFEFNLKP WDIAAGALIV QEAGGIVTDM SGEDGWLESG
DIVAANPKVL AQMLKIISAH V
