SUHB_XYLFT
ID SUHB_XYLFT Reviewed; 275 AA.
AC Q87BG1;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=PD_1493;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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}.
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DR EMBL; AE009442; AAO29337.1; -; Genomic_DNA.
DR RefSeq; WP_004088505.1; NC_004556.1.
DR AlphaFoldDB; Q87BG1; -.
DR SMR; Q87BG1; -.
DR EnsemblBacteria; AAO29337; AAO29337; PD_1493.
DR GeneID; 58017016; -.
DR KEGG; xft:PD_1493; -.
DR HOGENOM; CLU_044118_0_4_6; -.
DR OMA; VHQELEF; -.
DR Proteomes; UP000002516; 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..275
FT /note="Nus factor SuhB"
FT /id="PRO_0000142577"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 30206 MW; ED5F57BB22BA063A CRC64;
MQKPAVNIMV KAARSAGNVL LRHINKLETL HVIQKSRMDY ASDVDEMAEK VIVKELKRAY
PDYGILGEEG GLQGNHRIMW VIDPLDGTSN YLRGFPHYCV SIALVENGEP TDAVIFDPLR
NELFTASRGA GAVLNERKIR VANRKDLNGT MLNTGFSPRE RSRAHAQLKC VDALLMQAED
IRRSGSAALD LAYVACGRAD AYFEAGIKVW DVAAGMLLVR EAGGYVCDFK GADAPRMDDK
GPESCQLIAG NIKVAHALQQ VIVSSGYGRE FDPKR
