ID   SUHB_XYLFA              Reviewed;         275 AA.
AC   Q9PAM0;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 114.
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=XF_2476;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA   Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA   Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA   Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA   Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA   Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA   Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA   Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA   Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA   da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA   Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA   Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA   Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
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; AE003849; AAF85274.1; -; Genomic_DNA.
DR   PIR; E82554; E82554.
DR   RefSeq; WP_010894918.1; NC_002488.3.
DR   AlphaFoldDB; Q9PAM0; -.
DR   SMR; Q9PAM0; -.
DR   STRING; 160492.XF_2476; -.
DR   KEGG; xfa:XF_2476; -.
DR   eggNOG; COG0483; Bacteria.
DR   HOGENOM; CLU_044118_0_4_6; -.
DR   Proteomes; UP000000812; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:InterPro.
DR   GO; GO:0052834; F:inositol monophosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0006020; P:inositol metabolic process; IEA:TreeGrafter.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:TreeGrafter.
DR   CDD; cd01639; IMPase; 1.
DR   FunFam; 3.30.540.10:FF:000017; Inositol-1-monophosphatase; 1.
DR   FunFam; 3.40.190.80:FF:000002; 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   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..275
FT                   /note="Nus factor SuhB"
FT                   /id="PRO_0000142576"
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;  30234 MW;  74F622ACC4EE082C CRC64;
     MQKPAVNIMV KAARSAGNVL LRHINKLETL HVIQKSRMDY ASDVDEMAEK VIVKELKRAY
     PEYGILGEEG GLQGNHRIMW VIDPLDGTSN YLRGFPHYCI SIALVENGEP TDAVIFDPLR
     NELFTASRGA GAILNERKIR VANRKDLNGT MLNTGFSPRE RSRAHAQLKC VDALLMQAED
     IRRSGSAALD LAYVACGRAD AYFEAGIKVW DVAAGMLLVR EAGGYVCDFK GADAPRMDDK
     GPESCQLVAG NIKVAHALQQ VIVSSGYGRE FDPKR
//