SUHB_PSEAE
ID SUHB_PSEAE Reviewed; 271 AA.
AC Q9HXI4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Nus factor SuhB;
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;
GN Name=suhB {ECO:0000303|PubMed:24169572}; OrderedLocusNames=PA3818;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
RX PubMed=24169572; DOI=10.1128/mbio.00419-13;
RA Li K., Xu C., Jin Y., Sun Z., Liu C., Shi J., Chen G., Chen R., Jin S.,
RA Wu W.;
RT "SuhB is a regulator of multiple virulence genes and essential for
RT pathogenesis of Pseudomonas aeruginosa.";
RL MBio 4:E00419-E00419(2013).
RN [3]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAK;
RX PubMed=26179141; DOI=10.1111/mmi.13126;
RA Shi J., Jin Y., Bian T., Li K., Sun Z., Cheng Z., Jin S., Wu W.;
RT "SuhB is a novel ribosome associated protein that regulates expression of
RT MexXY by modulating ribosome stalling in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 98:370-383(2015).
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 -!- FUNCTION: A ribosome-associated protein, deletion of which alters the
CC expression of 494 genes, suggesting a role in global gene regulation
CC (PubMed:26179141). Involved in control of pathogenesis-related genes.
CC Required for the activation of virulence factors associated with acute
CC infections (type 3 secretion system, T3SS) while suppressing virulence
CC factors associated with chronic infections (biofilm formation and type
CC 6 secretion system, T6SS). It probably acts at a post-transcriptional
CC level (PubMed:24169572). {ECO:0000269|PubMed:24169572,
CC ECO:0000269|PubMed:26179141}.
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 (By similarity). Interacts with the
CC ribosome and with RNA polymerase (PubMed:26179141).
CC {ECO:0000250|UniProtKB:P0ADG4, ECO:0000269|PubMed:26179141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0ADG4}.
CC -!- INDUCTION: Transcription is strongly induced during mouse infection.
CC {ECO:0000269|PubMed:24169572}.
CC -!- DISRUPTION PHENOTYPE: Decreased expression of T3SS genes and effectors.
CC Loss of cytoxicity against human lung cell line A549, avirulent in a
CC mouse infection model. Down-regulation of flagellar genes and up-
CC regulation of T6SS structural genes and effectors, increased biofilm
CC formation (PubMed:24169572). Grows less quickly at 37 degrees Celsius.
CC Decreased susceptibility to antibiotics neomycin, streptomycin,
CC gentamycin, spectinomycin, ciprofloxacin and ofloxacin. Increased
CC ribosome stalling on leader peptide PA5471.1 mRNA, leads to increased
CC expression of PA5471 and up-regulation of the MexXY efflux system
CC (PubMed:26179141). {ECO:0000269|PubMed:24169572,
CC ECO:0000269|PubMed:26179141}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG07205.1; -; Genomic_DNA.
DR PIR; C83169; C83169.
DR RefSeq; NP_252507.1; NC_002516.2.
DR RefSeq; WP_003092845.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXI4; -.
DR SMR; Q9HXI4; -.
DR STRING; 287.DR97_4051; -.
DR PaxDb; Q9HXI4; -.
DR PRIDE; Q9HXI4; -.
DR DNASU; 879908; -.
DR EnsemblBacteria; AAG07205; AAG07205; PA3818.
DR GeneID; 879908; -.
DR KEGG; pae:PA3818; -.
DR PATRIC; fig|208964.12.peg.3997; -.
DR PseudoCAP; PA3818; -.
DR HOGENOM; CLU_044118_0_4_6; -.
DR InParanoid; Q9HXI4; -.
DR OMA; RVDGYWE; -.
DR PhylomeDB; Q9HXI4; -.
DR BioCyc; PAER208964:G1FZ6-3889-MON; -.
DR Proteomes; UP000002438; 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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding; Transcription;
KW Transcription antitermination; Transcription regulation; Virulence.
FT CHAIN 1..271
FT /note="Nus factor SuhB"
FT /id="PRO_0000142569"
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 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 88..91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0ADG4"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 271 AA; 29522 MW; EE1D43CFFEB871EA CRC64;
MQPMLNIALR AARSAGELIF RSIERLDVIS VNEKDAKDYV TEVDRAAEQT IVAALRKAYP
THAIMGEEGG FIEGSGEGAD YLWVIDPLDG TTNFIHGVPH FAVSIACKYK GRLEHAVVLD
PVRQEEFTAS RGRGAALNGR RLRVSGRKSL EGALLGTGFP FRDNQIDNLD NYLNMFRSLV
GQTAGIRRAG AASLDLAYVA AGRYDAFWEF GLSEWDMAAG ALLVQEAGGL VSDFTGSHEF
LEKGHIVAGN TKCFKALLTT IQPHLPPSLK R
