SUHB_BURCJ
ID SUHB_BURCJ Reviewed; 267 AA.
AC B4ED80;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Putative 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 {ECO:0000303|PubMed:22767545}; ORFNames=BCAL2157;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K56-2, and MH1K;
RX PubMed=22767545; DOI=10.1099/mic.0.060988-0;
RA Rosales-Reyes R., Saldias M.S., Aubert D.F., El-Halfawy O.M., Valvano M.A.;
RT "The suhB gene of Burkholderia cenocepacia is required for protein
RT secretion, biofilm formation, motility and polymyxin B resistance.";
RL Microbiology 158:2315-2324(2012).
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: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 -!- DISRUPTION PHENOTYPE: Grows more slowly than wild-type at 30 and 37
CC degrees Celsius, has defective protein secretion, swarming motility and
CC biofilm formation. Increased susceptibility to polymyxin B and SDS but
CC not to kanamycin or gentamycin. No change in the ability of bacteria to
CC infect macrophages. {ECO:0000269|PubMed:22767545}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM747720; CAR52459.1; -; Genomic_DNA.
DR RefSeq; WP_006493635.1; NC_011000.1.
DR AlphaFoldDB; B4ED80; -.
DR SMR; B4ED80; -.
DR STRING; 216591.BCAL2157; -.
DR EnsemblBacteria; CAR52459; CAR52459; BCAL2157.
DR GeneID; 56558656; -.
DR KEGG; bcj:BCAL2157; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_0_4; -.
DR OMA; VHQELEF; -.
DR OrthoDB; 1741160at2; -.
DR BioCyc; BCEN216591:G1G1V-2370-MON; -.
DR Proteomes; UP000001035; Chromosome 1.
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..267
FT /note="Putative Nus factor SuhB"
FT /id="PRO_0000451745"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
SQ SEQUENCE 267 AA; 29504 MW; 4EA262FE1D059561 CRC64;
MHPMLNIAVK AARRAGQIIN RASLDLDLIE IRKKQQNDFV TEVDKAAEDA IIETLKTAYP
DHAILAEESG ESDNESEFKW IIDPLDGTTN FIHGFPYYCV SIALEHKGVV TQAVVYDPNK
NDLFTATRGR GAYLNDRRIR VGRRDRLADA LVGTGFPFRE KDGLDAYARL FTEMTQACTG
LRRPGAAALD LANVAAGRLD AFFEQGINVW DMAAGSLLIT EAGGLVGNYT GDADFLHRHE
IVAANPKIYA QMIPILNRYS RVHPAAE
